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SBMC_SALTY
ID   SBMC_SALTY              Reviewed;         155 AA.
AC   P0A212; P41781;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=DNA gyrase inhibitor {ECO:0000255|HAMAP-Rule:MF_01896};
GN   Name=sbmC {ECO:0000255|HAMAP-Rule:MF_01896}; Synonyms=gyrI;
GN   OrderedLocusNames=STM2061;
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 [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   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
RC   STRAIN=LT2;
RX   PubMed=7737516; DOI=10.1016/0378-1119(94)00930-q;
RA   Alami N., Hallenbeck P.C.;
RT   "Cloning and characterization of a gene cluster, phsBCDEF, necessary for
RT   the production of hydrogen sulfide from thiosulfate by Salmonella
RT   typhimurium.";
RL   Gene 156:53-57(1995).
RN   [3]
RP   IDENTIFICATION.
RA   Robison K.;
RL   Unpublished observations (APR-1995).
CC   -!- FUNCTION: Inhibits the supercoiling activity of DNA gyrase. Acts by
CC       inhibiting DNA gyrase at an early step, prior to (or at the step of)
CC       binding of DNA by the gyrase. It protects cells against toxins that
CC       target DNA gyrase, by inhibiting activity of these toxins and reducing
CC       the formation of lethal double-strand breaks in the cell.
CC       {ECO:0000255|HAMAP-Rule:MF_01896}.
CC   -!- SUBUNIT: Interacts with DNA gyrase. {ECO:0000255|HAMAP-Rule:MF_01896}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01896}.
CC   -!- SIMILARITY: Belongs to the DNA gyrase inhibitor family.
CC       {ECO:0000255|HAMAP-Rule:MF_01896}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=L31538; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AE006468; AAL20965.1; -; Genomic_DNA.
DR   EMBL; L31538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_461006.1; NC_003197.2.
DR   RefSeq; WP_000384326.1; NC_003197.2.
DR   AlphaFoldDB; P0A212; -.
DR   SMR; P0A212; -.
DR   STRING; 99287.STM2061; -.
DR   PaxDb; P0A212; -.
DR   EnsemblBacteria; AAL20965; AAL20965; STM2061.
DR   GeneID; 1253582; -.
DR   KEGG; stm:STM2061; -.
DR   PATRIC; fig|99287.12.peg.2183; -.
DR   HOGENOM; CLU_113664_3_2_6; -.
DR   OMA; TPWYQFF; -.
DR   PhylomeDB; P0A212; -.
DR   BioCyc; SENT99287:STM2061-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008657; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) inhibitor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:2000372; P:negative regulation of DNA topoisomerase (ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.80.10; -; 1.
DR   HAMAP; MF_01896; DNA_gyrase_inhibitor; 1.
DR   InterPro; IPR010499; AraC_E-bd.
DR   InterPro; IPR024911; DNA_gyrase_inhibitor_GyrI.
DR   InterPro; IPR029442; GyrI-like.
DR   InterPro; IPR011256; Reg_factor_effector_dom_sf.
DR   Pfam; PF06445; GyrI-like; 1.
DR   SMART; SM00871; AraC_E_bind; 1.
DR   SUPFAM; SSF55136; SSF55136; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Reference proteome; Stress response.
FT   CHAIN           1..155
FT                   /note="DNA gyrase inhibitor"
FT                   /id="PRO_0000083884"
FT   CONFLICT        61..64
FT                   /note="EKLR -> GPAS (in Ref. 2; L31538)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   155 AA;  18062 MW;  FA14963A5EFE1DFD CRC64;
     MDYEIRQEQK RKIAGFHMVG PWEHTVKQGF EQLMTWVDRQ RIVPVEWIAV YYDNPDVVPA
     EKLRCDTVVS VAENFILPDN SEGVIVTAIE GGEYATAVAR VEDRDFAKPW ERFFDVLEQD
     SAYQIASAPC FETYLNNGME DGYWDIEMYI PVQRK
 
 
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