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SGRR_SALPA
ID   SGRR_SALPA              Reviewed;         552 AA.
AC   Q5PDG5;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=HTH-type transcriptional regulator SgrR {ECO:0000255|HAMAP-Rule:MF_01449};
GN   Name=sgrR {ECO:0000255|HAMAP-Rule:MF_01449}; OrderedLocusNames=SPA0111;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
CC   -!- FUNCTION: Activates the small RNA gene sgrS under glucose-phosphate
CC       stress conditions as well as yfdZ. Represses its own transcription
CC       under both stress and non-stress conditions. Might act as a sensor of
CC       the intracellular accumulation of phosphoglucose by binding these
CC       molecules in its C-terminal solute-binding domain. {ECO:0000255|HAMAP-
CC       Rule:MF_01449}.
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DR   EMBL; CP000026; AAV76144.1; -; Genomic_DNA.
DR   RefSeq; WP_001139028.1; NC_006511.1.
DR   AlphaFoldDB; Q5PDG5; -.
DR   SMR; Q5PDG5; -.
DR   EnsemblBacteria; AAV76144; AAV76144; SPA0111.
DR   KEGG; spt:SPA0111; -.
DR   HOGENOM; CLU_017028_12_3_6; -.
DR   OMA; WLTWQAE; -.
DR   Proteomes; UP000008185; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01449; HTH_type_SgrR; 1.
DR   InterPro; IPR039424; SBP_5.
DR   InterPro; IPR000914; SBP_5_dom.
DR   InterPro; IPR025370; SgrR_HTH_N.
DR   InterPro; IPR023767; Tscrpt_reg_SgrR.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR30290; PTHR30290; 1.
DR   Pfam; PF00496; SBP_bac_5; 1.
DR   Pfam; PF12793; SgrR_N; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
PE   3: Inferred from homology;
KW   Activator; DNA-binding; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..552
FT                   /note="HTH-type transcriptional regulator SgrR"
FT                   /id="PRO_0000309248"
FT   DOMAIN          1..116
FT                   /note="HTH marR-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01449"
FT   DNA_BIND        26..49
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01449"
FT   REGION          163..493
FT                   /note="Solute-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01449"
SQ   SEQUENCE   552 AA;  64038 MW;  9772CC4667B4C688 CRC64;
     MPSGRLQQQF IRLWQCCDGK TQDTTLNELA DLLNCSRRHM RTLLNTMQAR GWLTWEAEVG
     RGKRSRLTFL YTGLALQQQR AEDLLEQDRI DQLVQLVGDK SAVRQMLISH LGRSFRQGRH
     ILRVLYYRPM HNLLPGTALR RSETHIARQI FSSLTRVNEE NGELEADIAH HWQQISPLLW
     RFYLRPGIHF HHGRELEMED VIASLTRINT LPLYSHITKI DSPTAWTLDI HLSQPDRWLP
     WLLGQVPAMI LPREWETLAN FASHPIGTGP YAVRRNTPNQ LKILAFDDYF GYRALIDEVN
     VWVLPDISEE PACGLMLEGP IQGGEKAIES RLEEGCYYLL FDARTPRGAH PQVREWVSHV
     LSPTNLLYHA DEPLQQLWFP AYGLLPRWHH ARPGPGEKPA GLETLTLTFY REHIEHRVIA
     RIMSALLAEH QVHLHIQEID YDQWHAGEIE SDIWLNSANF TLPLDFSLFA HLCEVPLLQN
     CIPRDWQDDA AQWRAGEMNL ANWCQQLLAN KAIVPLIHHW LIIQGQRSMR GLRMNTLGWF
     DFKSAWFAPP DP
 
 
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