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RHO_SALTY
ID   RHO_SALTY               Reviewed;         419 AA.
AC   P0A295; P26980; Q93V24;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=STM3917;
GN   ORFNames=STMD1.73;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-163.
RC   STRAIN=LT2;
RX   PubMed=1561103; DOI=10.1093/nar/20.6.1424;
RA   Kotani H., Nakajima K.;
RT   "Cloning and sequence of thioredoxin gene of Salmonella typhimurium LT2.";
RL   Nucleic Acids Res. 20:1424-1424(1992).
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.
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; Z21789; CAA79852.1; -; Genomic_DNA.
DR   EMBL; AF233324; AAF33470.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL22766.1; -; Genomic_DNA.
DR   EMBL; D10015; BAA00904.1; -; Genomic_DNA.
DR   PIR; B49917; B49917.
DR   RefSeq; NP_462807.1; NC_003197.2.
DR   RefSeq; WP_001054532.1; NC_003197.2.
DR   AlphaFoldDB; P0A295; -.
DR   SMR; P0A295; -.
DR   STRING; 99287.STM3917; -.
DR   PaxDb; P0A295; -.
DR   EnsemblBacteria; AAL22766; AAL22766; STM3917.
DR   GeneID; 1255443; -.
DR   GeneID; 66758203; -.
DR   KEGG; stm:STM3917; -.
DR   PATRIC; fig|99287.12.peg.4138; -.
DR   HOGENOM; CLU_016377_4_3_6; -.
DR   OMA; TRLCRAH; -.
DR   PhylomeDB; P0A295; -.
DR   BioCyc; SENT99287:STM3917-MON; -.
DR   Proteomes; UP000001014; 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_0000188977"
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"
FT   CONFLICT        55
FT                   /note="L -> V (in Ref. 1; CAA79852)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   419 AA;  46993 MW;  C21C239CA27AEA84 CRC64;
     MNLTELKNTP VSELITLGES MGLENLARMR KQDIIFAILK QHAKSGEDIF GDGVLEILQD
     GFGFLRSADS SYLAGPDDIY VSPSQIRRFN LRTGDTISGK IRPPKEGERY FALLKVNEVN
     YDKPENARNK ILFENLTPLH ANSRLRMERG NGSTEDLTAR VLDLASPIGR GQRGLIVAPP
     KAGKTMLLQN IAQSIAYNHP DCVLMVLLID ERPEEVTEMQ RLVKGEVVAS TFDEPASRHV
     QVAEMVIEKA KRLVEHKKDV IILLDSITRL ARAYNTVVPA SGKVLTGGVD ANALHRPKRF
     FGAARNVEEG GSLTIIATAL IDTGSKMDEV IYEEFKGTGN MELHLSRKIA EKRVFPAIDY
     NRSGTRKEEL LTTQEELQKM WILRKIIHPM GEIDAMEFLI NKLAMTKTND DFFEMMKRS
 
 
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