RHO_ALLVD
ID RHO_ALLVD Reviewed; 418 AA.
AC P52152; D3RPH2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 115.
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=Alvin_0604;
OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS 10441 / D) (Chromatium vinosum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Allochromatium.
OX NCBI_TaxID=572477;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8051015; DOI=10.1128/jb.176.16.5033-5043.1994;
RA Opperman T., Richardson J.P.;
RT "Phylogenetic analysis of sequences from diverse bacteria with homology to
RT the Escherichia coli rho gene.";
RL J. Bacteriol. 176:5033-5043(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX PubMed=22675582; DOI=10.4056/sigs.2335270;
RA Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL Stand. Genomic Sci. 5:311-330(2011).
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}.
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DR EMBL; L27275; AAA59207.1; -; Genomic_DNA.
DR EMBL; CP001896; ADC61554.1; -; Genomic_DNA.
DR RefSeq; WP_012969830.1; NC_013851.1.
DR AlphaFoldDB; P52152; -.
DR SMR; P52152; -.
DR STRING; 572477.Alvin_0604; -.
DR PRIDE; P52152; -.
DR EnsemblBacteria; ADC61554; ADC61554; Alvin_0604.
DR KEGG; alv:Alvin_0604; -.
DR eggNOG; COG1158; Bacteria.
DR HOGENOM; CLU_016377_4_3_6; -.
DR OMA; TRLCRAH; -.
DR OrthoDB; 1619125at2; -.
DR Proteomes; UP000001441; 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; Reference proteome;
KW RNA-binding; Transcription; Transcription regulation;
KW Transcription termination.
FT CHAIN 1..418
FT /note="Transcription termination factor Rho"
FT /id="PRO_0000188960"
FT DOMAIN 48..123
FT /note="Rho RNA-BD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01203"
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 CONFLICT 56
FT /note="E -> EK (in Ref. 1; AAA59207)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="S -> L (in Ref. 1; AAA59207)"
FT /evidence="ECO:0000305"
FT CONFLICT 399..418
FT /note="LHDKLKATKTNDEFFSSMKG -> DIKLIDTVDQHRIGGFQNLFFERVIGHM
FT DDAIAH (in Ref. 1; AAA59207)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 418 AA; 46554 MW; 2EDDAABFBB70950D CRC64;
MNLTELKKMP VPNLVALAQS MDIEGVGRSR KQDLIFAILK AQAKKGEDIY GDGVLEILSD
GFGFLRSADA SYLAGPDDIY VSPSQIRRFA LRTGDTISGK IRPPKDGERY FALLKVNDIN
FDRPENAKSK ILFENFTPLF AQKRLTLEIG NGSTEDITAR TIDLVAPIGK GQRGLIVSPP
KAGKTMMLQN IAQSIGHNHP DCYLIVLLID ERPEEVTEMA RSVRGEVISS TFDEPATRHV
QVAEMVIEKA KRLVEHKRDV VILLDSITRL ARAYNTVVPS SGKVLTGGVD ANALQRPKRF
FGAARNVEEG GSLTILATAL VDTGSRMDDV IYEEFKGTGN MEIHMDRRIA EKRIFPAINI
NRSGTRREEL LMGQAELQKM WILRKILHPM DELAAMEFLH DKLKATKTND EFFSSMKG
