parC:Gene Product(s)

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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]

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Notes

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

Function

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<protect> 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]


</protect>

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]


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Notes

Structure and Physical Properties

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<protect> 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>

</protect>

Structure figures

<protect>

</protect>

Notes

Gene Product Resources

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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]

<protect></protect>

Notes

Accessions in Other Databases

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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

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Notes

Links

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References

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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

Categories

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