ID   RHO_NEIGO               Reviewed;         419 AA.
AC   Q06447;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 100.
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   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8253691; DOI=10.1128/jb.175.24.8030-8037.1993;
RA   Miloso M., Limauro D., Alifano P., Rivellini F., Lavitola A., Gulletta E.,
RA   Bruni C.B.;
RT   "Characterization of the rho genes of Neisseria gonorrhoeae and Salmonella
RT   typhimurium.";
RL   J. Bacteriol. 175:8030-8037(1993).
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; Z21790; CAA79853.1; -; Genomic_DNA.
DR   PIR; D49917; D49917.
DR   AlphaFoldDB; Q06447; -.
DR   SMR; Q06447; -.
DR   PRIDE; Q06447; -.
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_0000188972"
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"
SQ   SEQUENCE   419 AA;  47360 MW;  965077E82AAB5C76 CRC64;
     MHVSELQTLH ISKLLELAEE HGIENANRFR KQDLVFAIVR QMMKKGEGFT CSGTLEILPD
     GFGFLRSADT SYLAGPDDIY VSPTQIRRFN LHTGDTIEGS VRVPKDNERY FALVRLDSIN
     GDHPEVCRHK ILFENLTPLF PTEQLKLERD LKSEENLTGR AIDLISPIGK GQRALLVAPP
     KIGKTVMLEN IAHEVTANYP EVELIVLLID ERPEEVTEMS RSVRGEVVSS TFDEPAQRHV
     QVAEMVLEKA KRMVEHKKDV VILLDSITRL ARAYNTVVPA SGKILTGGVD ANALHRPKRF
     FGAARNVEEG GSLTIIATAL VETGSRMDDV IYEEFKGTGN MELHLDRRIA EKRLFPAINI
     NKSGTRREEL LVPNDQLQRM WLLRKFLHPM DEIEATEFLN GKIKASKNND DFFELMRGK