RHO_ECOL6
ID RHO_ECOL6 Reviewed; 419 AA.
AC P0AG31; P03002; Q48357;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Transcription termination factor Rho {ECO:0000255|HAMAP-Rule:MF_01884};
DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_01884};
DE AltName: Full=ATP-dependent helicase Rho {ECO:0000255|HAMAP-Rule:MF_01884};
GN Name=rho {ECO:0000255|HAMAP-Rule:MF_01884}; OrderedLocusNames=c4702;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Facilitates transcription termination by a mechanism that
CC involves Rho binding to the nascent RNA, activation of Rho's RNA-
CC dependent ATPase activity, and release of the mRNA from the DNA
CC template. {ECO:0000255|HAMAP-Rule:MF_01884}.
CC -!- SUBUNIT: Homohexamer. The homohexamer assembles into an open ring
CC structure. {ECO:0000255|HAMAP-Rule:MF_01884}.
CC -!- SIMILARITY: Belongs to the Rho family. {ECO:0000255|HAMAP-
CC Rule:MF_01884}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN83135.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014075; AAN83135.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_001054527.1; NC_004431.1.
DR AlphaFoldDB; P0AG31; -.
DR SMR; P0AG31; -.
DR STRING; 199310.c4702; -.
DR EnsemblBacteria; AAN83135; AAN83135; c4702.
DR GeneID; 67414430; -.
DR KEGG; ecc:c4702; -.
DR eggNOG; COG1158; Bacteria.
DR HOGENOM; CLU_016377_4_3_6; -.
DR OMA; TRLCRAH; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008186; F:ATP-dependent activity, acting on RNA; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-UniRule.
DR CDD; cd04459; Rho_CSD; 1.
DR CDD; cd01128; rho_factor; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01884; Rho; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR011129; CSD.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041703; Rho_factor_ATP-bd.
DR InterPro; IPR011112; Rho_N.
DR InterPro; IPR036269; Rho_N_sf.
DR InterPro; IPR011113; Rho_RNA-bd.
DR InterPro; IPR004665; Term_rho.
DR PANTHER; PTHR46425; PTHR46425; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF07498; Rho_N; 1.
DR Pfam; PF07497; Rho_RNA_bind; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00357; CSP; 1.
DR SMART; SM00959; Rho_N; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF68912; SSF68912; 1.
DR TIGRFAMs; TIGR00767; rho; 1.
DR PROSITE; PS51856; RHO_RNA_BD; 1.
PE 3: Inferred from homology;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; RNA-binding;
KW Transcription; Transcription regulation; Transcription termination.
FT CHAIN 1..419
FT /note="Transcription termination factor Rho"
FT /id="PRO_0000188964"
FT DOMAIN 48..123
FT /note="Rho RNA-BD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01203"
FT REGION 61..66
FT /note="RNA-binding 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT REGION 78..80
FT /note="RNA-binding 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT REGION 108..110
FT /note="RNA-binding 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT REGION 284..288
FT /note="RNA-binding 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT BINDING 169..174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT BINDING 181..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT BINDING 212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT SITE 326
FT /note="RNA-binding 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
SQ SEQUENCE 419 AA; 47004 MW; 5970A85334C43467 CRC64;
MNLTELKNTP VSELITLGEN MGLENLARMR KQDIIFAILK QHAKSGEDIF GDGVLEILQD
GFGFLRSADS SYLAGPDDIY VSPSQIRRFN LRTGDTISGK IRPPKEGERY FALLKVNEVN
FDKPENARNK ILFENLTPLH ANSRLRMERG NGSTEDLTAR VLDLASPIGR GQRGLIVAPP
KAGKTMLLQN IAQSIAYNHP DCVLMVLLID ERPEEVTEMQ RLVKGEVVAS TFDEPASRHV
QVAEMVIEKA KRLVEHKKDV IILLDSITRL ARAYNTVVPA SGKVLTGGVD ANALHRPKRF
FGAARNVEEG GSLTIIATAL IDTGSKMDEV IYEEFKGTGN MELHLSRKIA EKRVFPAIDY
NRSGTRKEEL LTTQEELQKM WILRKIIHPM GEIDAMEFLI NKLAMTKTND DFFEMMKRS
