ID RHO_HELPY Reviewed; 438 AA.
AC P56466;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 27-MAR-2024, entry version 141.
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=HP_0550;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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; AE000511; AAD07616.1; -; Genomic_DNA.
DR PIR; F64588; F64588.
DR RefSeq; NP_207345.1; NC_000915.1.
DR RefSeq; WP_001004715.1; NC_018939.1.
DR AlphaFoldDB; P56466; -.
DR SMR; P56466; -.
DR DIP; DIP-3446N; -.
DR IntAct; P56466; 4.
DR MINT; P56466; -.
DR STRING; 85962.HP_0550; -.
DR PaxDb; 85962-C694_02845; -.
DR EnsemblBacteria; AAD07616; AAD07616; HP_0550.
DR KEGG; hpy:HP_0550; -.
DR PATRIC; fig|85962.47.peg.595; -.
DR eggNOG; COG1158; Bacteria.
DR InParanoid; P56466; -.
DR OrthoDB; 9805197at2; -.
DR PhylomeDB; P56466; -.
DR Proteomes; UP000000429; Chromosome.
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; 1.10.720.10; -; 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; Reference proteome;
KW RNA-binding; Transcription; Transcription regulation;
KW Transcription termination.
FT CHAIN 1..438
FT /note="Transcription termination factor Rho"
FT /id="PRO_0000188966"
FT DOMAIN 70..145
FT /note="Rho RNA-BD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01203"
FT BINDING 188..193
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT BINDING 200..205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT BINDING 231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
SQ SEQUENCE 438 AA; 49547 MW; D4D06E6CD1E300F6 CRC64;
MNENAPTHKS SHKVKTHTPV SGYHIEDLRT YPTEKLLEIA NKLKVENPQE FKRQDLMFEI
LKTQVTQGGY ILFTGILEIM PDGYGFLRGF DGSFSDGHND TYVSPSQIRR FALRNGDIVT
GQVRSPKDQE KYYALLKIEA INYSPSDEIR NRPLFDNLTP LFPDEQIKLE YEPTKVTGRM
LDLFSPVGKG QRALIVAPPR TGKTELMKEL AQGITSNHPE VELIILLVDE RPEEVTDMQR
SVKGQVFSST FDLPANNHIR IAELVLERAK RRVEMGKDVV VLLDSITRLA RAYNAVTPSS
GKVLSGGVDA NALHRPKRFF GAARNIEEGG SLTIIATALI ETGSRMDEVI FEEFKGTGNS
EIVLARNIAD RRIYPAFDIL KSGTRKDNIL LGKDRLTKVW VLRNVMQQMD DIEALSFVYS
KMQQTKDNEE FLNLMNEK
//
