ECOLI:RHO

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	rho (synonyms: nitA, psuA, rnsC, sbaA, tsu)
Protein Name(s)	Transcription termination factor Rho ATP-dependent helicase Rho
External Links
UniProt	P0AG30
EMBL	J01673 M87049 U00096 AP009048 M12779 S75640 L34404
PIR	A03530
RefSeq	NP_418230.1 YP_491656.1
PDB	1A62 1A63 1A8V 1PV4 1PVO 1XPO 1XPR 1XPU 2A8V 2HT1 3ICE
PDBsum	1A62 1A63 1A8V 1PV4 1PVO 1XPO 1XPR 1XPU 2A8V 2HT1 3ICE
ProteinModelPortal	P0AG30
SMR	P0AG30
DIP	DIP-35363N
IntAct	P0AG30
MINT	MINT-1222551
STRING	511145.b3783
PaxDb	P0AG30
PRIDE	P0AG30
EnsemblBacteria	AAC76788 BAE77515
GeneID	12930703 948297
KEGG	ecj:Y75_p3392 eco:b3783
PATRIC	32123057
EchoBASE	EB0838
EcoGene	EG10845
eggNOG	COG1158
HOGENOM	HOG000076952
InParanoid	P0AG30
KO	K03628
OMA	DYNYLPG
OrthoDB	EOG6N681W
PhylomeDB	P0AG30
BioCyc	EcoCyc:EG10845-MONOMER ECOL316407:JW3756-MONOMER
EvolutionaryTrace	P0AG30
PRO	PR:P0AG30
Proteomes	UP000000318 UP000000625
Genevestigator	P0AG30
GO	GO:0016020 GO:0005524 GO:0004386 GO:0042802 GO:0003723 GO:0008186 GO:0006353 GO:0006355 GO:0006351
Gene3D	2.40.50.140 3.40.50.300
HAMAP	MF_01884
InterPro	IPR003593 IPR000194 IPR011129 IPR012340 IPR027417 IPR011112 IPR011113 IPR004665
Pfam	PF00006 PF07498 PF07497
SMART	SM00382 SM00357 SM00959
SUPFAM	SSF50249 SSF52540 SSF68912
TIGRFAMs	TIGR00767

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
part_of	GO:0016020	membrane	PMID:16858726^[1]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:24561554^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0AG30	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16858726^[1]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0AG30	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:15642265^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0AG30	F	Seeded From UniProt	complete
involved_in	GO:0006353	DNA-templated transcription, termination	PMID:7509071^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006351	transcription, DNA-templated	PMID:16669631^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:18304323^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:15911532^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:7509071^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003676	nucleic acid binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR011129	F	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004665 InterPro:IPR011113	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000194 InterPro:IPR004665	F	Seeded From UniProt	complete
involved_in	GO:0006353	DNA-templated transcription, termination	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004665 InterPro:IPR011112 InterPro:IPR011113	P	Seeded From UniProt	complete
enables	GO:0008186	RNA-dependent ATPase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004665	F	Seeded From UniProt	complete
involved_in	GO:0006353	DNA-templated transcription, termination	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000087053	P	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000087053	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000087053	F	Seeded From UniProt	complete
enables	GO:0004386	helicase activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000087053	F	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F	Seeded From UniProt	complete
involved_in	GO:0006353	DNA-templated transcription, termination	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0806	P	Seeded From UniProt	complete
enables	GO:0004386	helicase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0347	F	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0694	F	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F	Seeded From UniProt	complete
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Notes

References

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

↑ ^1.0 ^1.1 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
↑ Rajagopala, SV et al. (2014) The binary protein-protein interaction landscape of Escherichia coli. Nat. Biotechnol. 32 285-90 PubMed GONUTS page
↑ Skordalakes, E et al. (2005) Structural mechanism of inhibition of the Rho transcription termination factor by the antibiotic bicyclomycin. Structure 13 99-109 PubMed GONUTS page
↑ ^4.0 ^4.1 Steinmetz, EJ & Platt, T (1994) Evidence supporting a tethered tracking model for helicase activity of Escherichia coli Rho factor. Proc. Natl. Acad. Sci. U.S.A. 91 1401-5 PubMed GONUTS page
↑ Walmacq, C et al. (2006) Testing the steric exclusion model for hexameric helicases: substrate features that alter RNA-DNA unwinding by the transcription termination factor Rho. Biochemistry 45 5885-95 PubMed GONUTS page
↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page

[PMID:16858726-1] 1.0 ^1.1 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page

[PMID:24561554-2] Rajagopala, SV et al. (2014) The binary protein-protein interaction landscape of Escherichia coli. Nat. Biotechnol. 32 285-90 PubMed GONUTS page

[PMID:15642265-3] Skordalakes, E et al. (2005) Structural mechanism of inhibition of the Rho transcription termination factor by the antibiotic bicyclomycin. Structure 13 99-109 PubMed GONUTS page

[PMID:7509071-4] 4.0 ^4.1 Steinmetz, EJ & Platt, T (1994) Evidence supporting a tethered tracking model for helicase activity of Escherichia coli Rho factor. Proc. Natl. Acad. Sci. U.S.A. 91 1401-5 PubMed GONUTS page

[PMID:16669631-5] Walmacq, C et al. (2006) Testing the steric exclusion model for hexameric helicases: substrate features that alter RNA-DNA unwinding by the transcription termination factor Rho. Biochemistry 45 5885-95 PubMed GONUTS page

[PMID:18304323-6] Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

[PMID:15911532-7] Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page

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ECOLI:RHO

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