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ICLR_SALTY
ID   ICLR_SALTY              Reviewed;         274 AA.
AC   P17430;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Acetate operon repressor;
GN   Name=iclR; OrderedLocusNames=STM4187;
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].
RX   PubMed=2194169; DOI=10.1093/nar/18.12.3656;
RA   Galinier A., Negre D., Cortay J.-C., Marcandier S., Maloy S.R.,
RA   Cozzone A.J.;
RT   "Sequence analysis of the iclR gene encoding the repressor of the acetate
RT   operon in Salmonella typhimurium.";
RL   Nucleic Acids Res. 18:3656-3656(1990).
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).
CC   -!- FUNCTION: Regulation of the glyoxylate bypass operon, which encodes
CC       isocitrate lyase, malate synthase as well as isocitrate dehydrogenase
CC       kinase/phosphorylase.
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DR   EMBL; X52950; CAA37126.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL23011.1; -; Genomic_DNA.
DR   PIR; S12729; S12729.
DR   RefSeq; NP_463052.1; NC_003197.2.
DR   RefSeq; WP_000226434.1; NC_003197.2.
DR   AlphaFoldDB; P17430; -.
DR   SMR; P17430; -.
DR   STRING; 99287.STM4187; -.
DR   PaxDb; P17430; -.
DR   EnsemblBacteria; AAL23011; AAL23011; STM4187.
DR   GeneID; 1255713; -.
DR   KEGG; stm:STM4187; -.
DR   PATRIC; fig|99287.12.peg.4400; -.
DR   HOGENOM; CLU_062618_7_1_6; -.
DR   OMA; EPDRLHR; -.
DR   PhylomeDB; P17430; -.
DR   BioCyc; SENT99287:STM4187-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR014757; Tscrpt_reg_IclR_C.
DR   InterPro; IPR005471; Tscrpt_reg_IclR_N.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF09339; HTH_IclR; 1.
DR   Pfam; PF01614; IclR; 1.
DR   SMART; SM00346; HTH_ICLR; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS51077; HTH_ICLR; 1.
DR   PROSITE; PS51078; ICLR_ED; 1.
PE   4: Predicted;
KW   DNA-binding; Glyoxylate bypass; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..274
FT                   /note="Acetate operon repressor"
FT                   /id="PRO_0000201759"
FT   DOMAIN          24..86
FT                   /note="HTH iclR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00393"
FT   DOMAIN          101..272
FT                   /note="IclR-ED"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00394"
FT   DNA_BIND        46..65
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00393"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         160..161
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000250"
FT   BINDING         212
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000250"
FT   BINDING         222
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000250"
FT   BINDING         239..241
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        43
FT                   /note="S -> T (in Ref. 1; CAA37126)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        59
FT                   /note="T -> S (in Ref. 1; CAA37126)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        86
FT                   /note="A -> P (in Ref. 1; CAA37126)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        152..157
FT                   /note="GKLPMH -> ASCPMP (in Ref. 1; CAA37126)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        205
FT                   /note="R -> A (in Ref. 1; CAA37126)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        244
FT                   /note="C -> R (in Ref. 1; CAA37126)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   274 AA;  29614 MW;  0A860F6107C95C92 CRC64;
     MVAPVPAKRG RKPAATTAPV TGQVQSLTRG LKLLEWIAES NGSVALTELA QQAGLPNSTT
     HRLLTTMQQQ GFVRQVGELG HWAVGAHAFI VGSSFLQSRN LLAIVHPILR KLMEDSGETV
     NLAVLDQSDH QAIIIDQVQC TQLMRMSAPI GGKLPMHASG AGKAFLSQLS EEQVTSLLHR
     KGLHAYTHAT LVSPLHLKDD LAQTRKRGYS FDDEEHALGL RCVASCIYDE HREPFAALSI
     SGPCSRITDD RVTELGAMVI KAAKEVTLAY GGTR
 
 
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