ID   RHO_PSEFC               Reviewed;         419 AA.
AC   P52155;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 91.
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};
OS   Pseudomonas fluorescens biotype C.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=335;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 17400 / DSM 50117 / ICPB 2656-18 / NBRC 15833 / NCIMB 10460 /
RC   Stanier C-18;
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).
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; L27278; AAA59209.1; -; Genomic_DNA.
DR   AlphaFoldDB; P52155; -.
DR   SMR; P52155; -.
DR   PRIDE; P52155; -.
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_0000188973"
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;  46954 MW;  ED30BDE6ACE03253 CRC64;
     MNLTELKQKP ITDLLQLAEE MGIENMARSR KQDVIFSLLK KHAKSGEEIS GDGVLEILQD
     GFGFLRSADA SYLAGPDDIY VSPSQIRRFN LRTGDTIVGK IRPPKEGERY FALLKVDTIN
     FDRPENAKNK ILFENLTPLF PTVRMKMEAG NGSTEDLTGR VIDLCAPIGK GQRGLIVAPP
     KAGKTIMLQN IAANIARNNP EVHLIVLLID ERPEEVTEMQ RTVRGEVVAS TFDEPPTRHV
     QVAEMVIEKA KRLVEHKKDV VILLDSITRL ARAYNTVIPS SGKVLTGGVD AHALEKPKRF
     FGAARNIEEG GSLTIIATAL VETGSKMDEV IYEEFKGTGN MELPLDRRIA EKRVFPAINI
     NRSGTRREEL LTADDELQRM WILRKLLHPM DEVAAIEFLI DKLKTTKTND EFFLSMKRK