rng:Gene Product(s)

From EcoliWiki
Revision as of 05:00, 22 May 2009 by 127.0.0.1 (talk) (Data loaded by TableEdit_Loader.)
Jump to navigation Jump to search

{{#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

Rng

Synonyms

ribonuclease G[1], B3247[2][1], AdhR[2][1], Rng[2][1], YhdF[2][1], CafA[2][1]

Product description

ribonuclease G (RNAse G)[2][3];

Component of ribonuclease G (RNAse G)[3]

Endoribonuclease G involved in 16S rRNA processing; division and growth, overexpression forms minicells and chains with long axial structures[4]

EC number (for enzymes)
edit table


Notes

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(s) Evidence Code with/from Aspect Notes Status
GO:0008996

ribonuclease G activity

PMID:10722715[5]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0006364

rRNA processing

PMID:10362534[7]

IMP: Inferred from Mutant Phenotype

P

Seeded from EcoCyc 12.5 [6]

complete

GO:0051301

cell division

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0132

P

Seeded from EcoCyc [8]

complete

GO:0016787

hydrolase activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0378

F

Seeded from EcoCyc [8]

complete

GO:0007049

cell cycle

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0131

P

Seeded from EcoCyc [8]

complete

GO:0006396

RNA processing

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004659

P

Seeded from EcoCyc [8]

complete

GO:0005856

cytoskeleton

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0206

C

Seeded from EcoCyc [8]

complete

GO:0008996

ribonuclease G activity

PMID:10722715[5]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc [8]

complete

GO:0004540

ribonuclease activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004659

F

Seeded from EcoCyc [8]

complete

GO:0004519

endonuclease activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0255

F

Seeded from EcoCyc [8]

complete

GO:0006364

rRNA processing

PMID:10362534[7]

IMP: Inferred from Mutant Phenotype

P

Seeded from EcoCyc [8]

complete

GO:0003723

RNA binding

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR003029

F

Seeded from EcoCyc [8]

complete

GO:0005515

protein binding

PMID:15690043[9]

IPI: Inferred from Physical Interaction

UniProtKB:P0A7V8

F

Seeded from EcoCyc [8]

complete

GO:0003723

RNA binding

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR003029

F

Seeded from EcoCyc

complete

GO:0004518

nuclease activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0540

F

Seeded from EcoCyc

complete

GO:0004519

endonuclease activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0255

F

Seeded from EcoCyc

complete

GO:0004540

ribonuclease activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004659

F

Seeded from EcoCyc

complete

GO:0006364

rRNA processing

PMID:10362534[7]

IMP: Inferred from Mutant Phenotype

P

Seeded from EcoCyc

complete

GO:0005737

cytoplasm

GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR004659
SP_KW:KW-0963

C

Seeded from EcoCyc

complete

GO:0005856

cytoskeleton

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0206

C

Seeded from EcoCyc

complete

GO:0006396

RNA processing

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004659

P

Seeded from EcoCyc

complete

NOT

GO:0009451

RNA modification

P

Seeded from EcoCyc 11.1[3].

I think this annotation is incorrect. RNA modification is The covalent alteration of one or more nucleotides within an RNA molecule to produce an RNA molecule with a sequence that differs from that coded genetically." Rng processes 16S RNA, but I could find no evidence that it modifies the sequence.

required field missing

GO:0006401

RNA catabolic process

P

Seeded from EcoCyc 11.1[3].

I think this annotation is incorrect because processing by Rng is involved in the synthesis of functional ribosomes not the turnover of ribosomes (DAS, TAMU).

required field missing

NOT

GO:0000910

cytokinesis

P

Seeded from EcoCyc 11.1[3].

Overproduction of CafA causes a cell division defect: chains of cells and minicells form when expression of cafA from a multicopy plasmid is induced by the addition of IPTG [10]/>. Long axial filaments were also observed to form. (DAS, TAMU)

required field missing

GO:0008996

ribonuclease G activity

PMID:10722715[5]

IDA: Inferred from Direct Assay

F

complete

GO:0006364

rRNA processing

PMID:10362534[7]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0007049

cell cycle

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0131

P

Seeded from EcoCyc

complete

edit table

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 ribonuclease G (RNAse G)

could be indirect

Protein

rpsD

PMID:15690043[9]

Experiment(s):EBI-890107

Protein

rplB

PMID:16606699[11]

Experiment(s):EBI-1145286

Protein

rpsI

PMID:16606699[11]

Experiment(s):EBI-1145286

Protein

rpsC

PMID:16606699[11]

Experiment(s):EBI-1145286

Protein

rpsB

PMID:16606699[11]

Experiment(s):EBI-1145286

Protein

rplQ

PMID:16606699[11]

Experiment(s):EBI-1145286

Protein

racC

PMID:16606699[11]

Experiment(s):EBI-1145286

Protein

dnaK

PMID:15690043[9]

Experiment(s):EBI-895082

Protein

eno

PMID:15690043[9]

Experiment(s):EBI-895082

Protein

rpe

PMID:15690043[9]

Experiment(s):EBI-895082

Protein

rpsE

PMID:15690043[9]

Experiment(s):EBI-895082

Protein

rpsI

PMID:15690043[9]

Experiment(s):EBI-895082

Protein

rpsM

PMID:15690043[9]

Experiment(s):EBI-895082

Protein

rpsO

PMID:15690043[9]

Experiment(s):EBI-895082

Protein

rpsS

PMID:15690043[9]

Experiment(s):EBI-895082

Protein

rpsT

PMID:15690043[9]

Experiment(s):EBI-895082

Protein

rpsU

PMID:15690043[9]

Experiment(s):EBI-895082

edit table


Notes

Localization

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

Compartment Description Evidence Notes

cytoplasm

From EcoCyc[3]

edit table


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.

Sequence

at EcoCyc

MRKGINMTAE LLVNVTPSET RVAYIDGGIL QEIHIEREAR RGIVGNIYKG RVSRVLPGMQ
AAFVDIGLDK AAFLHASDIM PHTECVAGEE QKQFTVRDIS ELVRQGQDLM VQVVKDPLGT
KGARLTTDIT LPSRYLVFMP GASHVGVSQR IESESERERL KKVVAEYCDE QGGFIIRTAA
EGVGEAELAS DAAYLKRVWT KVMERKKRPQ TRYQLYGELA LAQRVLRDFA DAELDRIRVD
SRLTYEALLE FTSEYIPEMT SKLEHYTGRQ PIFDLFDVEN EIQRALERKV ELKSGGYLII
DQTEAMTTVD INTGAFVGHR NLDDTIFNTN IEATQAIARQ LRLRNLGGII IIDFIDMNNE
DHRRRVLHSL EQALSKDRVK TSVNGFSALG LVEMTRKRTR ESIEHVLCNE CPTCHGRGTV
KTVETVCYEI MREIVRVHHA YDSDRFLVYA SPAVAEALKG EESHSLAEVE IFVGKQVKVQ
IEPLYNQEQF DVVMM
Length

495

Mol. Wt

55.36 kDa (calc) [2]

pI
Extinction coefficient

27850 - 28600 (calc based on 15 Y, 1 W, and 6 C residues)

edit table


Domains/Motifs/Modification Sites

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

Type Residues Description Notes

Domain

39 - 128

S1 motif

UniProt:P0A9J0

edit table

<motif_map/>

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

Structures

<beststructure>rng 562</beststructure>

Models

View models at:

edit table


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
edit table


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

EcoCyc (EcoliWiki Page)

EcoCyc:EG11299-MONOMER

UniProt (EcoliWiki Page)

UniProt:P0A9J0

PFAM (EcoliWiki Page)

PFAM:PF00575

RefSeq (EcoliWiki Page)

RefSeq:NP_417713


edit table


Notes

Links

[back to top]


Name URL Comments
edit table



References

[back to top]


  1. ↑ 1.0 1.1 1.2 1.3 1.4 1.5 1.6 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 2.3 2.4 2.5 2.6 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 3.3 3.4 3.5 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. ↑ 5.0 5.1 5.2 Tock, MR et al. (2000) The CafA protein required for the 5'-maturation of 16 S rRNA is a 5'-end-dependent ribonuclease that has context-dependent broad sequence specificity. J. Biol. Chem. 275 8726-32 PubMed
  6. ↑ 6.0 6.1 EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  7. ↑ 7.0 7.1 7.2 7.3 Wachi, M et al. (1999) Escherichia coli cafA gene encodes a novel RNase, designated as RNase G, involved in processing of the 5' end of 16S rRNA. Biochem. Biophys. Res. Commun. 259 483-8 PubMed
  8. ↑ 8.00 8.01 8.02 8.03 8.04 8.05 8.06 8.07 8.08 8.09 8.10 EcoCyc (release 13.0; 2009) Keseler, IM et al. (2009) Nucleic Acids Res. 37(Database issue):D464-70
  9. ↑ 9.00 9.01 9.02 9.03 9.04 9.05 9.06 9.07 9.08 9.09 9.10 9.11 Butland, G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433 531-7 PubMed
  10. ↑ Okada, Y et al. (1994) Cytoplasmic axial filaments in Escherichia coli cells: possible function in the mechanism of chromosome segregation and cell division. J. Bacteriol. 176 917-22 PubMed
  11. ↑ 11.0 11.1 11.2 11.3 11.4 11.5 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed


Categories

[back to top]