ID   RHO_RICCN               Reviewed;         458 AA.
AC   Q92HL2;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 122.
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=RC0759;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
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; AE006914; AAL03297.1; -; Genomic_DNA.
DR   PIR; G97794; G97794.
DR   RefSeq; WP_004998383.1; NC_003103.1.
DR   AlphaFoldDB; Q92HL2; -.
DR   SMR; Q92HL2; -.
DR   GeneID; 927486; -.
DR   KEGG; rco:RC0759; -.
DR   HOGENOM; CLU_016377_4_3_5; -.
DR   Proteomes; UP000000816; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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: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_C; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR00767; rho; 1.
DR   PANTHER; PTHR46425; TRANSCRIPTION TERMINATION FACTOR RHO; 1.
DR   PANTHER; PTHR46425:SF1; TRANSCRIPTION TERMINATION FACTOR RHO; 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; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF68912; Rho N-terminal domain-like; 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_0000286651"
FT   DOMAIN          78..153
FT                   /note="Rho RNA-BD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01203"
FT   REGION          1..23
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;  51278 MW;  6D65C3DA7FD244D6 CRC64;
     MNTTNKESTA ELNNTESNNN YNNFAENGNI INLKQLKRKL PEELQAQAEE LKIENINSLL
     KQELVFAILK KSVEQGVLIV GEGVLEVLPD GFGFLRSPEV NYLAGPDDIY ISPSQIRRFG
     LRTGDTVEGQ IRAPKAGERY FALLKVNRVN FEDPSKAYHR VHFDNLTPLY PDEKLGLELE
     NNSKDSKDFS TRVIELVAPM GKGQRALIVA PPRTGKTVLL QNIAHAITTN NPEVFLIVLL
     IDERPEEVTD MQRSVRGEVV SSTFDEPASR HVQLAEMVIK KAKRLVEHKK DVVILVDAIT
     RLARAYNTVV PSSGKVLTGG VDANALQRPK RFFGAARNIE NGGSLTIIGT ALIETGSRMD
     EVIFEEFKGT GNSEIVLDRK IADKRIYPAI DITRSGTRKE DLLVDKIILN KMWVLRRIID
     PMGSSEAIEF LLKKLENTKT NGEFFEMMKS PERPKNGL
//