RHO_RICFE
ID RHO_RICFE Reviewed; 458 AA.
AC Q4ULF7;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=RF_0765;
OS Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=315456;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-1525 / URRWXCal2;
RX PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA Parinello H., Claverie J.-M., Raoult D.;
RT "The genome sequence of Rickettsia felis identifies the first putative
RT conjugative plasmid in an obligate intracellular parasite.";
RL PLoS Biol. 3:1-12(2005).
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; CP000053; AAY61616.1; -; Genomic_DNA.
DR RefSeq; WP_011271094.1; NC_007109.1.
DR AlphaFoldDB; Q4ULF7; -.
DR SMR; Q4ULF7; -.
DR STRING; 315456.RF_0765; -.
DR EnsemblBacteria; AAY61616; AAY61616; RF_0765.
DR KEGG; rfe:RF_0765; -.
DR eggNOG; COG1158; Bacteria.
DR HOGENOM; CLU_016377_4_3_5; -.
DR OMA; TRLCRAH; -.
DR OrthoDB; 1619125at2; -.
DR Proteomes; UP000008548; 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..458
FT /note="Transcription termination factor Rho"
FT /id="PRO_0000286652"
FT DOMAIN 78..153
FT /note="Rho RNA-BD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01203"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 201..206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT BINDING 213..218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT BINDING 244
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
SQ SEQUENCE 458 AA; 51269 MW; 840CAC28B46115A7 CRC64;
MNTTNKESTE ELNNTESNNN HNNFAENGNI INLKQLKRKL PEELQAQAEE LKIENINSLL
KQELVFAILK KSVEQGGLIV GEGVLEVLPD GFGFLRSPEV NYLAGPDDIY ISPSQIRRFG
LRTGDTVEGQ IRAPKAGERY FALLKVNRVN FEDPSKAYHR VHFDNLTPLY PDEKLGLELE
NNSKDSKDFS TRVIELVAPM GKGQRALIVA PPRTGKTVLL QNIAHAITTN NPEVFLIVLL
IDERPEEVTD MQRSVRGEVV SSTFDEPASR HVQLAEMVIE KAKRLVEHKK DVVILVDAIT
RLARAYNTVV PSSGKVLTGG VDANALQRPK RFFGAARNIE NGGSLTIIGT ALIETGSRMD
EVIFEEFKGT GNSEIVLDRK IADKRIYPAI DITRSGTRKE DLLVDKIILN KMWVLRRIID
PMGSSEAIEF LLKKLENTKT NGEFFEMMKS PERPKNGL