UniProt Accession

 RHO_ECOLI; P0AG30; P03002; Q2M891; Q48357 

Genbank Protein ID

 J01673; M87049; U00096; AP009048; M12779; S75640; L34404 

Genbank Nucleotide ID

 AAA24532.1; AAA67583.1; AAC76788.1; BAE77515.1; AAA24695.1; AAB20841.1; AAA68985.1 

Protein Name

 Transcription termination factor Rho 

Protein Synonyms/Alias

 ATP-dependent helicase Rho 

Gene Name

 rho 

Gene Synonyms/Alias

 nitA; psuA; rnsC; sbaA; tsu; b3783; JW3756 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
31	ENLARMRKQDIIFAI	acetylation	[1]
40	DIIFAILKQHAKSGE	acetylation	[1]
100	TGDTISGKIRPPKEG	acetylation	[1]
105	SGKIRPPKEGERYFA	acetylation	[1]
115	ERYFALLKVNEVNFD	acetylation	[1, 2, 3]
123	VNEVNFDKPENARNK	acetylation	[1]
130	KPENARNKILFENLT	acetylation	[1]
224	TEMQRLVKGEVVAST	acetylation	[1, 3]
249	VAEMVIEKAKRLVEH	acetylation	[1]
258	KRLVEHKKDVIILLD	acetylation	[1]
283	TVVPASGKVLTGGVD	acetylation	[1]
298	ANALHRPKRFFGAAR	acetylation	[1]
367	YNRSGTRKEELLTTQ	acetylation	[1]
379	TTQEELQKMWILRKI	acetylation	[1]
385	QKMWILRKIIHPMGE	acetylation	[1, 3]
402	AMEFLINKLAMTKTN	acetylation	[1]
407	INKLAMTKTNDDFFE	acetylation	[1]
417	DDFFEMMKRS*****	acetylation	[1]

Reference

 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [2] The diversity of lysine-acetylated proteins in Escherichia coli.
 Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG.
 J Microbiol Biotechnol. 2008 Sep;18(9):1529-36. [PMID: 18852508]
 [3] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111] 

Functional Description

 Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template. RNA-dependent NTPase which utilizes all four ribonucleoside triphosphates as substrates. 

Sequence Annotation

 NP_BIND 169 174 ATP (Potential).
 NP_BIND 181 186 ATP.
 REGION 61 66 RNA-binding 1.
 REGION 78 80 RNA-binding 1.
 REGION 108 110 RNA-binding 1.
 REGION 284 288 RNA-binding 2.
 BINDING 212 212 ATP.  

Keyword

 3D-structure; ATP-binding; Complete proteome; Direct protein sequencing; Helicase; Hydrolase; Nucleotide-binding; Reference proteome; RNA-binding; Transcription; Transcription regulation; Transcription termination. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 419 AA 

Protein Sequence

Gene Ontology

 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0004386; F:helicase activity; IEA:HAMAP.
 GO:0003723; F:RNA binding; IDA:EcoCyc.
 GO:0008186; F:RNA-dependent ATPase activity; IEA:InterPro.
 GO:0006353; P:DNA-dependent transcription, termination; IDA:EcoCyc.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW. 

Interpro

 IPR003593; AAA+_ATPase.
 IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
 IPR011129; Cold_shock_prot.
 IPR012340; NA-bd_OB-fold.
 IPR027417; P-loop_NTPase.
 IPR011112; Rho_N.
 IPR011113; Rho_RNA-bd.
 IPR004665; Term_rho. 

Pfam

 PF00006; ATP-synt_ab
 PF07498; Rho_N
 PF07497; Rho_RNA_bind 

SMART

 SM00382; AAA
 SM00357; CSP
 SM00959; Rho_N 

PROSITE

  

PRINTS