parC:Gene Product(s): Difference between revisions

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!align=left {{table heading style}} |Synonyms
!align=left {{table heading style}} |Synonyms
||
||
DNA topoisomerase IV, subunit A<ref name='LIB:Riley_2006'/>, B3019<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, ParC<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>  
''DNA topoisomerase IV, subunit A<ref name='LIB:Riley_2006'/>, B3019<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, ParC<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/> , ECK3010, JW2987, b3019''
 
Category:Complex:topoisomerase IV
|-
|-
!align=left {{table heading style}} |Product description
!align=left {{table heading style}} |Product description
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topoisomerase IV subunit A<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;  
topoisomerase IV subunit A<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;  


Component of [[:Category:Complex:dimer of topoisomerase IV subunit A|dimer of topoisomerase IV subunit A]]<ref name='LIB:EcoCyc11.1'/>; [[:Category:Complex:topoisomerase IV|topoisomerase IV]]<ref name='LIB:EcoCyc11.1'/>
Component of [[Topoisomerase IV]]<ref name='LIB:EcoCyc11.1'/>


Topoisomerase IV, subunit A, ATP-dependent, type II; chromosome decatenase; relaxes both positive and negative supercoils; DNA unknotting activity; heterotetrameric<ref name='LIB:EcoGene'/>
Topoisomerase IV, subunit A, ATP-dependent, type II; chromosome decatenase; relaxes both positive and negative supercoils; DNA unknotting activity; heterotetrameric<ref name='LIB:EcoGene'/>
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<protect><!--Nomenclature_notes--></protect>
<protect><!--Nomenclature_notes--></protect>
===Notes===
===Notes===
 
More information about the Topo IV complex may be found on the [[Topoisomerase IV]] page.


==Function==
==Function==
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*  
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{| {{Prettytable}} id="P46aacca09a6d8"  class=" tableEdit GO_table_product dataTable"   
{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="P46aacca09a6d8"  class=" tableEdit GO_table_product dataTable"   
|- {{table_heading_style}}
|- {{table_heading_style}}
!|Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
!|Qualifier!!GO ID!!GO term name!!Reference!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-  
|-  
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PMID:8104339
PMID:8104339
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IDA: Inferred from Direct Assay
IDA: Inferred from Direct Assay
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*  
*  
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{|   id="A46aaccac8541e"  class=" tableEdit Product_interactions_table dataTable"   
{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"  id="A46aaccac8541e"  class=" tableEdit Product_interactions_table dataTable"   
|- {{table heading style}}
|- {{table heading style}}
!|Partner Type!!Partner!!Notes!!References!!Evidence
!|Partner Type!!Partner!!Notes!!References!!Evidence
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Subunits of [[:Category:Complex:dimer of topoisomerase IV subunit A|dimer of topoisomerase IV subunit A]]  
Subunits of [[:Category:Complex:dimer of topoisomerase IV subunit A|dimer of topoisomerase IV subunit A]]  
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could be indirect
 
|
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Protein
Protein
|
|
Subunits of [[:Category:Complex:topoisomerase IV|topoisomerase IV]]
murF
|
 
|
PMID:19402753
|
LCMS(ID Probability):99.0
|-
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Protein
|
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could be indirect
mreB
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|


|
|
PMID:19402753
|
MALDI(Z-score):33.310369
|-  
|-  
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Protein
Protein
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MreB
rplB
|
|


|
|
PMID:19187760
PMID:19402753
|
MALDI(Z-score):37.621172
|-
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Protein
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gyrA
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|


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PMID:19402753
|}
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MALDI(Z-score):26.844062
 
<!--Function_notes--></protect>
===Notes===
 
 
==Localization==
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!|Compartment!!Description!!Evidence!!Source!!Notes
|-  
|-  
|
|
cytoplasm
Protein
|
|
rfaQ
|
|
 
|
|
From EcoCyc<ref name='LIB:EcoCyc11.1'/>
PMID:19402753
|
LCMS(ID Probability):99.0
|-
|
Protein
|
rplL
|
|


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PMID:19402753
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<!--box uid=421aa90e079fa326b6494f812ad13e79.26428.Q46aaccae4a6a3-->
LCMS(ID Probability):99.6
|-
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Protein
|
Subunits of [[:Category:Complex:topoisomerase IV|topoisomerase IV]]
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could be indirect
|


<protect><!--Localization_notes--></protect>
|
 
===Notes===
|-  
 
|
==Structure and Physical Properties==
Protein
{{BacktoTop}}
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<protect>
MreB
<span id="Sequence"></span><big>'''Physical Properties'''</big>
|
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|-
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!align=left {{table heading style}} |Sequence
PMID:19187760
||
|
[http://biocyc.org/ECOLI/sequence-aa?object=EG10686-MONOMER at EcoCyc]
Purified MreB inhibits decatanation by Topo IV.  
<pre>MSDMAERLAL HEFTENAYLN YSMYVIMDRA LPFIGDGLKP VQRRIVYAMS ELGLNASAKF
|-  
KKSARTVGDV LGKYHPHGDS ACYEAMVLMA QPFSYRYPLV DGQGNWGAPD DPKSFAAMRY
|
TESRLSKYSE LLLSELGQGT ADWVPNFDGT LQEPKMLPAR LPNILLNGTT GIAVGMATDI
Protein
PPHNLREVAQ AAIALIDQPK TTLDQLLDIV QGPDYPTEAE IITSRAEIRK IYENGRGSVR
|
MRAVWKKEDG AVVISALPHQ VSGARVLEQI AAQMRNKKLP MVDDLRDESD HENPTRLVIV
FtsK
PRSNRVDMDQ VMNHLFATTD LEKSYRINLN MIGLDGRPAV KNLLEILSEW LVFRRDTVRR
|
RLNYRLEKVL KRLHILEGLL VAFLNIDEVI EIIRNEDEPK PALMSRFGLT ETQAEAILEL
FtsK stimulates Topo IV's decatenation activity ''in vitro''
KLRHLAKLEE MKIRGEQSEL EKERDQLQGI LASERKMNNL LKKELQADAQ AYGDDRRSPL
|
QEREEAKAMS EHDMLPSEPV TIVLSQMGWV RSAKGHDIDA PGLNYKAGDS FKAAVKGKSN
PMID:12939258
QPVVFVDSTG RSYAIDPITL PSARGQGEPL TGKLTLPPGA TVDHMLMESD DQKLLMASDA
|
GYGFVCTFND LVARNRAGKA LITLPENAHV MPPVVIEDAS DMLLAITQAG RMLMFPVSDL
*Two-hybrid analysis
PQLSKGKGNK IINIPSAEAA RGEDGLAQLY VLPPQSTLTI HVGKRKIKLR PEELQKVTGE
*Immunoblotting
RGRRGTLMRG LQRIDRVEID SPRRASSGDS EE</pre>
|-  
|-
|
!align=left {{table heading style}} |Length
Protein
||
|
752
MukB
|-
|
!align=left {{table heading style}} |Mol. Wt
 
||
|
83.833 kDa
PMID:20696938
|-
|
!align=left {{table heading style}} |pI
||
6.7 (calculated)
|-
!align=left {{table heading style}} |Extinction coefficient
||
55,810 - 56,060 (calc based on 19 Y, 5 W, and 2 C residues)


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<wikiPageContents>Image:1ZVU.pdb</wikiPageContents>
<!--Function_notes--></protect>
===Notes===




 
==Localization==
 
<!--box uid=421aa90e079fa326b6494f812ad13e79.26428.Q46aaccae4a6a3-->
<span id="Domains/Motifs/Modification Sites"><big>'''Domains/Motifs/Modification Sites'''</big></span><table>
<tr align="left" valign="top">
<td><!--box uid=421aa90e079fa326b6494f812ad13e79.26428.Z46aaccb05c8e6-->
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{|   id="Z46aaccb05c8e6"  class=" tableEdit Product_motif_table dataTable"   
{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"  id="Q46aaccae4a6a3"  class=" tableEdit Product_localization_table"   
|- {{table heading style}}
|- {{table heading style}}
!|Type!!Residues!!Description!!Notes!!References
!|Compartment!!Description!!Evidence!!Reference/Source!!Notes
|-  
|-  
|
|
Domain
cytoplasm
|
|
591..638
   
|
[http://pfam.janelia.org/family/PF03989 PF03989 DNA gyrase C-terminal domain, beta-propeller]
|
[http://pfam.janelia.org/protein/P0AFI2 Pfam:P0AFI2]
|
|
   
   
|-
|
|
Domain
From EcoCyc<ref name='LIB:EcoCyc11.1'/>
|
640..691
|
[http://pfam.janelia.org/family/PF03989 PF03989  DNA gyrase C-terminal domain, beta-propeller]
|
[http://pfam.janelia.org/protein/P0AFI2 Pfam:P0AFI2]
|
|-
|
Domain
|
29..466
|
[http://pfam.janelia.org/family/PF00521 PF00521  DNA gyrase/topoisomerase IV, subunit A]
|
[http://pfam.janelia.org/protein/P0AFI2 Pfam:P0AFI2]
|
|
   
   


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<td>
 
<!-- motifs column 2-->
<protect><!--Localization_notes--></protect>
<motif_map/>
</td>
</tr>
</table>


<table><tr valign='top'><td>
===Notes===
<span id='Structure'></span><big>'''Structure'''</big><br />
 
<!--box uid=421aa90e079fa326b6494f812ad13e79.26428.Y46aaccb0bb9e0-->
==Structure and Physical Properties==
{{BacktoTop}}
<protect>
<span id="Sequence"></span><big>'''Physical Properties'''</big>
<!--box uid=421aa90e079fa326b6494f812ad13e79.26428.Q46aaccafe0004-->
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{|  id="Y46aaccb0bb9e0"  class=" tableEdit Product_structure_table"   
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|-
|-
!align=left {{table heading style}} |Structures
!align=left {{table heading style}} |Name
||
||
<beststructure>
 
gene=parC
taxon=562,83333
</beststructure>
|-
|-
!align=left {{table heading style}} |Models
!align=left {{table heading style}} |Sequence
||
||
View models at:
[http://biocyc.org/ECOLI/sequence-aa?object=EG10686-MONOMER at EcoCyc]  
* [http://dragon.bio.purdue.edu/ecolpredict2/localsearch/cgi-bin/search3.cgi?q=recA EcoliPredict]
<pre>MSDMAERLAL HEFTENAYLN YSMYVIMDRA LPFIGDGLKP VQRRIVYAMS ELGLNASAKF
* [http://modbase.compbio.ucsf.edu/modbase-cgi/model_search.cgi?searchmode=default&displaymode=moddetail&searchproperties=ALL&searchvalue=recA&organism=562&organismtext= ModBase]
KKSARTVGDV LGKYHPHGDS ACYEAMVLMA QPFSYRYPLV DGQGNWGAPD DPKSFAAMRY
* [http://bioinf.cs.ucl.ac.uk/psipred/ PSI-PRED]
TESRLSKYSE LLLSELGQGT ADWVPNFDGT LQEPKMLPAR LPNILLNGTT GIAVGMATDI
* [http://www.ebi.ac.uk/msd-srv/pqs/ Protein Quaternary Structure] (PQS)
PPHNLREVAQ AAIALIDQPK TTLDQLLDIV QGPDYPTEAE IITSRAEIRK IYENGRGSVR
* [http://spock.genes.nig.ac.jp/~genome/search.html Genomes TO Protein] (GTOP)
MRAVWKKEDG AVVISALPHQ VSGARVLEQI AAQMRNKKLP MVDDLRDESD HENPTRLVIV
 
PRSNRVDMDQ VMNHLFATTD LEKSYRINLN MIGLDGRPAV KNLLEILSEW LVFRRDTVRR
|- class="tableEdit_footer"
RLNYRLEKVL KRLHILEGLL VAFLNIDEVI EIIRNEDEPK PALMSRFGLT ETQAEAILEL
|<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26428.Y46aaccb0bb9e0&page=26428&pagename={{FULLPAGENAMEE}}&type=1&template=Product_structure_table edit table]</span> ||
KLRHLAKLEE MKIRGEQSEL EKERDQLQGI LASERKMNNL LKKELQADAQ AYGDDRRSPL
|}
QEREEAKAMS EHDMLPSEPV TIVLSQMGWV RSAKGHDIDA PGLNYKAGDS FKAAVKGKSN
<!--box uid=421aa90e079fa326b6494f812ad13e79.26428.Y46aaccb0bb9e0-->
QPVVFVDSTG RSYAIDPITL PSARGQGEPL TGKLTLPPGA TVDHMLMESD DQKLLMASDA
 
GYGFVCTFND LVARNRAGKA LITLPENAHV MPPVVIEDAS DMLLAITQAG RMLMFPVSDL
{{Image:1ZVU.pdb}}
PQLSKGKGNK IINIPSAEAA RGEDGLAQLY VLPPQSTLTI HVGKRKIKLR PEELQKVTGE
 
RGRRGTLMRG LQRIDRVEID SPRRASSGDS EE</pre>
</td><td></protect>
|-
==== Structure figures ====
!align=left {{table heading style}} |Length
 
||
 
752
 
|-
 
!align=left {{table heading style}} |Mol. Wt
 
||
83.833 kDa
|-
!align=left {{table heading style}} |pI
||
6.7 (calculated)
|-
!align=left {{table heading style}} |Extinction coefficient
||
55,810 - 56,060 (calc based on 19 Y, 5 W, and 2 C residues)


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<span id="Domains/Motifs/Modification Sites"><big>'''Domains/Motifs/Modification Sites'''</big></span><table>
 
<tr align="left" valign="top">
 
<td><!--box uid=421aa90e079fa326b6494f812ad13e79.26428.Z46aaccb05c8e6-->
 
<!--
 
 
 
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</td><tr><table><!--Structure_notes--></protect>
===Notes===
 
 
==Gene Product Resources==
{{BacktoTop}}
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{|   id="X46aaccb23fe78"  class=" tableEdit Product_resource_table"   
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|- {{table_heading_style}}
|- {{table heading style}}
!|Type!!Residues!!Description!!Notes!!References
|-
|
Domain
|
591..638
|
[http://pfam.janelia.org/family/PF03989 PF03989  DNA gyrase C-terminal domain, beta-propeller]
|
 
|
PMID:19920124
|-
|
Domain
|
640..691
|
[http://pfam.janelia.org/family/PF03989 PF03989  DNA gyrase C-terminal domain, beta-propeller]
|
 
|
PMID:19920124
|-
|
Domain
|
29..466
|
[http://pfam.janelia.org/family/PF00521 PF00521  DNA gyrase/topoisomerase IV, subunit A]
|
 
|
PMID:19920124
 
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<td>
<!-- motifs column 2-->
<motif_map/>
</td>
</tr>
</table>
 
<table><tr valign='top'><td>
<span id='Structure'></span><big>'''Structure'''</big><br />
<!--box uid=421aa90e079fa326b6494f812ad13e79.26428.Y46aaccb0bb9e0-->
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|-
!align=left {{table heading style}} |Structures
||
<beststructure>
gene=parC
taxon=562,83333
</beststructure>
|-
!align=left {{table heading style}} |Models
||
View models at:
* [http://www.proteinmodelportal.org/query/uniprot/P0AFI2 Protein Model Portal]
* [http://bioinf.cs.ucl.ac.uk/genome3d/read?uniprot_id=P0AFI2 PSI-PRED (P0AFI2)]
* [http://spock.genes.nig.ac.jp/~genome/cgi-bin/gkeytext.pl.cgi?A&QUERY1=P0AFI2 Genomes TO Protein (P0AFI2)] (GTOP)
 
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{{Image:1ZVU.pdb}}
 
</td><td></protect>
==== Structure figures ====
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
<protect><!--          ***** PLEASE DO NOT EDIT BELOW THIS LINE *****        -->
</td><tr><table><!--Structure_notes--></protect>
===Notes===
 
 
==Gene Product Resources==
{{BacktoTop}}
<!--box uid=421aa90e079fa326b6494f812ad13e79.26428.X46aaccb23fe78-->
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|- {{table_heading_style}}
!|Resource type!!Source!!Notes/Reference
!|Resource type!!Source!!Notes/Reference
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<protect><!--Resources_notes--></protect>
===Notes===
==Accessions in Other Databases==
{{BacktoTop}}
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!|Database!!Accession!!Notes
|-  
|-  
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[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])  
Purification protocol
|
ParC(&Delta;CTD)
|
PMID:20081205
 
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<protect><!--Resources_notes--></protect>
===Notes===
 
 
==Accessions in Other Databases==
{{BacktoTop}}
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|- {{table_heading_style}}
!|Database!!Accession!!Notes
|-
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[http://www.ncbi.nlm.nih.gov/protein NCBI (Protein)] ([[NCBI (Protein)|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/protein/16130915 GI:16130915]
|
Escherichia coli str. K-12 substr. MG1655
|-
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[http://www.ncbi.nlm.nih.gov/protein NCBI (Protein)] ([[NCBI (Protein)|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/protein/NP_417491.1 GeneID:947499]
|
Escherichia coli str. K-12 substr. MG1655
|-
|
[[ASAP]]
|
ASAP:ABE-0009916
|
''Escherichia coli'' str. K-12 substr. [[:Category:Strain:MG1655|MG1655]]
|-
|
[http://www.pir.uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[http://www.uniprot.org/uniprot/P0AFI2 UniProtKB/Swiss-Prot:P0AFI2]
|
Escherichia coli str. K-12 substr. MG1655
|-
|
[[EcoCyc]]
|
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=EG10686-MONOMER EcoCyc:EG10686-MONOMER]
EcoCyc:EG10686
|
|
''Escherichia coli'' str. K-12 substr. [[:Category:Strain:MG1655|MG1655]]
|-  
|-  
|
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[http://swissmodel.expasy.org/repository/ SwissModel] ([[SwissModel|EcoliWiki Page]])
[[EcoGene]]
|
|
[http://swissmodel.expasy.org/repository/smr.php?job=2&sptr_ac=P0AFI2 SwissModel:P0AFI2]
EcoGene:EG10686
|
|
''Escherichia coli'' str. K-12 substr. [[:Category:Strain:MG1655|MG1655]]
|-  
|-  
|
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])  
[http://www.ncbi.nlm.nih.gov/gene NCBI (Gene)] ([[NCBI (Gene)|EcoliWiki Page]])
|
|
[[uniprot:P0AFI2|UniProt:P0AFI2]]
[http://www.ncbi.nlm.nih.gov/gene?term=947499 GeneID:947499]
|
|
Escherichia coli str. K-12 substr. MG1655
|-  
|-  
|
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[http://pfam.sanger.ac.uk/ PFAM] ([[PFAM|EcoliWiki Page]])
[[RegulonDB]]
|
|
[http://pfam.sanger.ac.uk/family?acc=PF00521 PFAM:PF00521]
RegulonDB:ECK120000679
|
|
''Escherichia coli'' str. K-12 substr. [[:Category:Strain:MG1655|MG1655]]
|-  
|-  
|
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
[[EchoBASE]]
|
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_417491 RefSeq:NP_417491]
EchoBASE:EB0680
|
|
''Escherichia coli'' str. K-12 substr. [[:Category:Strain:MG1655|MG1655]]


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[[Category:Proteins]]
[[Category:Proteins]]
[[Category:GO:0005737_!_cytoplasm]][[Category:GO:0006261_!_DNA-dependent DNA replication]][[Category:Complex:dimer of topoisomerase IV subunit A]][[Category:Complex:topoisomerase IV]][[Category:Location:cytoplasm]][[Category:Products with structures in PDB]]

Latest revision as of 20:58, 17 February 2015

{{#css:Suppresslinks.css}}<css>h1 .editsection { display:none;} h2 .editsection { display:none;}</css>

Quickview   Gene   Gene Product(s)   Expression   Evolution   On One Page    
Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

ParC

Synonyms

DNA topoisomerase IV, subunit A[1], B3019[2][1], ParC[2][1] , ECK3010, JW2987, b3019

Category:Complex:topoisomerase IV

Product description

topoisomerase IV subunit A[2][3];

Component of Topoisomerase IV[3]

Topoisomerase IV, subunit A, ATP-dependent, type II; chromosome decatenase; relaxes both positive and negative supercoils; DNA unknotting activity; heterotetrameric[4]

EC number (for enzymes)

5.99.1.-[1]


Notes

More information about the Topo IV complex may be found on the Topoisomerase IV page.

Function

[back to top]


Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0003918

DNA topoisomerase (ATP-hydrolyzing) activity

IDA: Inferred from Direct Assay

F

Missing: reference

GO:0007059

chromosome segregation

PMID:2842295[5]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0003677

DNA binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002205

F

Seeded from EcoCyc (v14.0)

complete

Contributes to

GO:0003916

DNA topoisomerase activity

PMID:1334483[6]

IDA: Inferred from Direct Assay

F

complete

GO:0003677

DNA binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005742

F

Seeded from EcoCyc (v14.0)

complete

GO:0019897

extrinsic to plasma membrane

PMID:1334483[6]

IDA: Inferred from Direct Assay

C

in the presence of DNA

complete

GO:0003677

DNA binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006691

F

Seeded from EcoCyc (v14.0)

complete

GO:0005737

cytoplasm

PMID:1334483[6]

IDA: Inferred from Direct Assay

C

in the presence of Mg2+

complete

GO:0003677

DNA binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013757

F

Seeded from EcoCyc (v14.0)

complete

Contributes to

GO:0003918

DNA topoisomerase (ATP-hydrolyzing) activity

PMID:8227000[7]

IDA: Inferred from Direct Assay

F

complete

GO:0003677

DNA binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013758

F

Seeded from EcoCyc (v14.0)

complete

GO:0009330

DNA topoisomerase complex (ATP-hydrolyzing)

PMID:8227000[7]

IDA: Inferred from Direct Assay

C

complete

GO:0006265

DNA topological change

PMID:8227000[7]

IDA: Inferred from Direct Assay

P

complete

GO:0003677

DNA binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013760

F

Seeded from EcoCyc (v14.0)

complete

GO:0003677

DNA binding

PMID:16023670[8]

IDA: Inferred from Direct Assay

F

complete

GO:0003677

DNA binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0238

F

Seeded from EcoCyc (v14.0)

complete

GO:0003916

DNA topoisomerase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006691

F

Seeded from EcoCyc (v14.0)

complete

GO:0030541

plasmid partitioning

PMID:8104339[9]

IDA: Inferred from Direct Assay

P

complete

GO:0003916

DNA topoisomerase activity

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0799

F

Seeded from EcoCyc (v14.0)

complete

GO:0003918

DNA topoisomerase (ATP-hydrolyzing) activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002205

F

Seeded from EcoCyc (v14.0)

complete

GO:0003918

DNA topoisomerase (ATP-hydrolyzing) activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005742

F

Seeded from EcoCyc (v14.0)

complete

GO:0003918

DNA topoisomerase (ATP-hydrolyzing) activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013757

F

Seeded from EcoCyc (v14.0)

complete

GO:0006265

DNA topological change

PMID:16023670[8]

IDA: Inferred from Direct Assay

P

complete

GO:0003918

DNA topoisomerase (ATP-hydrolyzing) activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013758

F

Seeded from EcoCyc (v14.0)

complete

GO:0007059

chromosome segregation

PMID:16023670[8]

IDA: Inferred from Direct Assay

P

complete

GO:0003918

DNA topoisomerase (ATP-hydrolyzing) activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013760

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002205

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005742

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006691

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013757

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013758

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013760

F

Seeded from EcoCyc (v14.0)

complete

GO:0005694

chromosome

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002205

C

Seeded from EcoCyc (v14.0)

complete

GO:0005694

chromosome

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005742

C

Seeded from EcoCyc (v14.0)

complete

GO:0005694

chromosome

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006691

C

Seeded from EcoCyc (v14.0)

complete

GO:0007062

sister chromatid cohesion

PMID:18765793[10]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0005694

chromosome

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013757

C

Seeded from EcoCyc (v14.0)

complete

GO:0005694

chromosome

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013758

C

Seeded from EcoCyc (v14.0)

complete

GO:0005694

chromosome

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013760

C

Seeded from EcoCyc (v14.0)

complete

GO:0006265

DNA topological change

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002205

P

Seeded from EcoCyc (v14.0)

complete

GO:0006265

DNA topological change

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005742

P

Seeded from EcoCyc (v14.0)

complete

GO:0006265

DNA topological change

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006691

P

Seeded from EcoCyc (v14.0)

complete

GO:0006265

DNA topological change

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013757

P

Seeded from EcoCyc (v14.0)

complete

GO:0006265

DNA topological change

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013758

P

Seeded from EcoCyc (v14.0)

complete

GO:0006265

DNA topological change

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013760

P

Seeded from EcoCyc (v14.0)

complete

GO:0016853

isomerase activity

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0413

F

Seeded from EcoCyc (v14.0)

complete

Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner Type Partner Notes References Evidence

Protein

Subunits of dimer of topoisomerase IV subunit A

Protein

yciH

PMID:16606699[11]

Experiment(s):EBI-1144556

Protein

rplB

PMID:16606699[11]

Experiment(s):EBI-1144556

Protein

rplA

PMID:16606699[11]

Experiment(s):EBI-1144556

Protein

pflD

PMID:16606699[11]

Experiment(s):EBI-1144556

Protein

aceF

PMID:15690043[12]

Experiment(s):EBI-883350

Protein

lpdA

PMID:15690043[12]

Experiment(s):EBI-883350

Protein

mreB

PMID:15690043[12]

Experiment(s):EBI-883350

Protein

gyrA

PMID:15690043[12]

Experiment(s):EBI-883350

Protein

secA

PMID:15690043[12]

Experiment(s):EBI-883350

Protein

murF

PMID:15690043[12]

Experiment(s):EBI-890645

Protein

rfaQ

PMID:15690043[12]

Experiment(s):EBI-890645

Protein

rplL

PMID:15690043[12]

Experiment(s):EBI-890645

Protein

rplM

PMID:15690043[12]

Experiment(s):EBI-890645

Protein

rplV

PMID:15690043[12]

Experiment(s):EBI-890645

Protein

rpmA

PMID:15690043[12]

Experiment(s):EBI-890645

Protein

rpmG

PMID:15690043[12]

Experiment(s):EBI-890645

Protein

rpsB

PMID:15690043[12]

Experiment(s):EBI-890645

Protein

rpsJ

PMID:15690043[12]

Experiment(s):EBI-890645

Protein

slyD

PMID:15690043[12]

Experiment(s):EBI-890645

Protein

murF

PMID:19402753[13]

LCMS(ID Probability):99.0

Protein

mreB

PMID:19402753[13]

MALDI(Z-score):33.310369

Protein

rplB

PMID:19402753[13]

MALDI(Z-score):37.621172

Protein

gyrA

PMID:19402753[13]

MALDI(Z-score):26.844062

Protein

rfaQ

PMID:19402753[13]

LCMS(ID Probability):99.0

Protein

rplL

PMID:19402753[13]

LCMS(ID Probability):99.6

Protein

Subunits of topoisomerase IV

could be indirect

Protein

MreB

PMID:19187760[14]

Purified MreB inhibits decatanation by Topo IV.

Protein

FtsK

FtsK stimulates Topo IV's decatenation activity in vitro

PMID:12939258[15]

  • Two-hybrid analysis
  • Immunoblotting

Protein

MukB

PMID:20696938[16]



Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

Compartment Description Evidence Reference/Source Notes

cytoplasm

From EcoCyc[3]



Notes

Structure and Physical Properties

[back to top]


Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Name
Sequence

at EcoCyc

MSDMAERLAL HEFTENAYLN YSMYVIMDRA LPFIGDGLKP VQRRIVYAMS ELGLNASAKF
KKSARTVGDV LGKYHPHGDS ACYEAMVLMA QPFSYRYPLV DGQGNWGAPD DPKSFAAMRY
TESRLSKYSE LLLSELGQGT ADWVPNFDGT LQEPKMLPAR LPNILLNGTT GIAVGMATDI
PPHNLREVAQ AAIALIDQPK TTLDQLLDIV QGPDYPTEAE IITSRAEIRK IYENGRGSVR
MRAVWKKEDG AVVISALPHQ VSGARVLEQI AAQMRNKKLP MVDDLRDESD HENPTRLVIV
PRSNRVDMDQ VMNHLFATTD LEKSYRINLN MIGLDGRPAV KNLLEILSEW LVFRRDTVRR
RLNYRLEKVL KRLHILEGLL VAFLNIDEVI EIIRNEDEPK PALMSRFGLT ETQAEAILEL
KLRHLAKLEE MKIRGEQSEL EKERDQLQGI LASERKMNNL LKKELQADAQ AYGDDRRSPL
QEREEAKAMS EHDMLPSEPV TIVLSQMGWV RSAKGHDIDA PGLNYKAGDS FKAAVKGKSN
QPVVFVDSTG RSYAIDPITL PSARGQGEPL TGKLTLPPGA TVDHMLMESD DQKLLMASDA
GYGFVCTFND LVARNRAGKA LITLPENAHV MPPVVIEDAS DMLLAITQAG RMLMFPVSDL
PQLSKGKGNK IINIPSAEAA RGEDGLAQLY VLPPQSTLTI HVGKRKIKLR PEELQKVTGE
RGRRGTLMRG LQRIDRVEID SPRRASSGDS EE
Length

752

Mol. Wt

83.833 kDa

pI

6.7 (calculated)

Extinction coefficient

55,810 - 56,060 (calc based on 19 Y, 5 W, and 2 C residues)

<wikiPageContents>Image:1ZVU.pdb</wikiPageContents>



Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

Type Residues Description Notes References

Domain

591..638

PF03989 DNA gyrase C-terminal domain, beta-propeller

PMID:19920124[17]

Domain

640..691

PF03989 DNA gyrase C-terminal domain, beta-propeller

PMID:19920124[17]

Domain

29..466

PF00521 DNA gyrase/topoisomerase IV, subunit A

PMID:19920124[17]

<motif_map/>

Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures

<beststructure> gene=parC taxon=562,83333 </beststructure>

Models

View models at:

See Help:Jmol in EcoliWiki

Text label
<jmol> <jmolApplet> <color>white</color> <uploadedFileContents >1ZVU.pdb</uploadedFileContents> <name></name> <script> wireframe off; spacefill off; trace off; rotate ON; cartoon; color chain; </script> </jmolApplet> </jmol>
<jmol> <jmolCheckbox > <scriptWhenChecked > rotate on; </scriptWhenChecked > <scriptWhenUnchecked > rotate off; </scriptWhenUnchecked > <checked>true</checked> <text>rotate</text> </jmolCheckbox > <jmolButton><script>reset; </script><text>reset</text></jmolButton> </jmol>

Structure figures

Notes

Gene Product Resources

[back to top]


See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference

Purification protocol

ParC(ΔCTD)

PMID:20081205[18]


Notes

Accessions in Other Databases

[back to top]


See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

NCBI (Protein) (EcoliWiki Page)

GI:16130915

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:947499

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0009916

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P0AFI2

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG10686

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG10686

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:947499

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120000679

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB0680

Escherichia coli str. K-12 substr. MG1655


Notes

Links

[back to top]




References

[back to top]


See Help:References for how to manage references in EcoliWiki.

  1. ↑ 1.0 1.1 1.2 1.3 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 3.0 3.1 3.2 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. ↑ Kato, J et al. (1988) Gene organization in the region containing a new gene involved in chromosome partition in Escherichia coli. J. Bacteriol. 170 3967-77 PubMed
  6. ↑ 6.0 6.1 6.2 Kato, J et al. (1992) Purification and characterization of DNA topoisomerase IV in Escherichia coli. J. Biol. Chem. 267 25676-84 PubMed
  7. ↑ 7.0 7.1 7.2 Peng, H & Marians, KJ (1993) Escherichia coli topoisomerase IV. Purification, characterization, subunit structure, and subunit interactions. J. Biol. Chem. 268 24481-90 PubMed
  8. ↑ 8.0 8.1 8.2 Corbett, KD et al. (2005) The structural basis for substrate specificity in DNA topoisomerase IV. J. Mol. Biol. 351 545-61 PubMed
  9. ↑ Peng, H & Marians, KJ (1993) Decatenation activity of topoisomerase IV during oriC and pBR322 DNA replication in vitro. Proc. Natl. Acad. Sci. U.S.A. 90 8571-5 PubMed
  10. ↑ Wang, X et al. (2008) Modulation of Escherichia coli sister chromosome cohesion by topoisomerase IV. Genes Dev. 22 2426-33 PubMed
  11. ↑ 11.0 11.1 11.2 11.3 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  12. ↑ 12.00 12.01 12.02 12.03 12.04 12.05 12.06 12.07 12.08 12.09 12.10 12.11 12.12 12.13 12.14 Butland, G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433 531-7 PubMed
  13. ↑ 13.0 13.1 13.2 13.3 13.4 13.5 Hu, P et al. (2009) Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins. PLoS Biol. 7 e96 PubMed
  14. ↑ Madabhushi, R & Marians, KJ (2009) Actin homolog MreB affects chromosome segregation by regulating topoisomerase IV in Escherichia coli. Mol. Cell 33 171-80 PubMed
  15. ↑ Espeli, O et al. (2003) A physical and functional interaction between Escherichia coli FtsK and topoisomerase IV. J. Biol. Chem. 278 44639-44 PubMed
  16. ↑ Hayama, R & Marians, KJ (2010) Physical and functional interaction between the condensin MukB and the decatenase topoisomerase IV in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 107 18826-31 PubMed
  17. ↑ 17.0 17.1 17.2 Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed
  18. ↑ Bigot, S & Marians, KJ (2010) DNA chirality-dependent stimulation of topoisomerase IV activity by the C-terminal AAA+ domain of FtsK. Nucleic Acids Res. 38 3031-40 PubMed

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