ID   RHO_BUCAI               Reviewed;         419 AA.
AC   P57652;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 121.
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=BU596;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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; BA000003; BAB13281.1; -; Genomic_DNA.
DR   RefSeq; NP_240395.1; NC_002528.1.
DR   RefSeq; WP_009874544.1; NC_002528.1.
DR   AlphaFoldDB; P57652; -.
DR   SMR; P57652; -.
DR   STRING; 107806.10039247; -.
DR   EnsemblBacteria; BAB13281; BAB13281; BAB13281.
DR   KEGG; buc:BU596; -.
DR   PATRIC; fig|107806.10.peg.599; -.
DR   eggNOG; COG1158; Bacteria.
DR   HOGENOM; CLU_016377_4_3_6; -.
DR   OMA; TRLCRAH; -.
DR   Proteomes; UP000001806; 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..419
FT                   /note="Transcription termination factor Rho"
FT                   /id="PRO_0000188957"
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;  46888 MW;  86907932A717B700 CRC64;
     MNLTALKNMP VSELITLGEK MGLENLARMR KQDIIFAILK QHAKSGEDIF GDGVLEILQD
     GFGFLRSADS SYLAGPDDIY VSPSQIRRFN LRTGDTIAGK IRPPKEGERY FALLKVNEVN
     YDKPENARSK ILFENLTPLH ANSRLRMERG NGSTEDLTAR VLDLASPIGR GQRGLIVAPP
     KAGKTILLQN IAQSIAYNHP DCVLMVLLID ERPEEVTEMQ RLVKGEVVAS TFDEPASRHV
     QVAEMVIEKA KRLVEHKKDV IILLDSITRL ARAYNTVVPA SGKVLTGGVD ANALHRPKRF
     FGAARNVEEG GSLTIIATAL VDTGSKMDEV IYEEFKGTGN MELPLSRKIA EKRVFPAIDY
     NRSGTRKEEL LTLPDELQKM WILRKIIHPM SEIDAMEFLL NKLAMTKTND EFFDMMKRS