ID   SBMC_YERE8              Reviewed;         157 AA.
AC   A1JN27;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=YE2070;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
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}.
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DR   EMBL; AM286415; CAL12144.1; -; Genomic_DNA.
DR   RefSeq; WP_011816334.1; NC_008800.1.
DR   RefSeq; YP_001006315.1; NC_008800.1.
DR   AlphaFoldDB; A1JN27; -.
DR   SMR; A1JN27; -.
DR   STRING; 393305.YE2070; -.
DR   EnsemblBacteria; CAL12144; CAL12144; YE2070.
DR   KEGG; yen:YE2070; -.
DR   PATRIC; fig|393305.7.peg.2235; -.
DR   eggNOG; COG3449; Bacteria.
DR   HOGENOM; CLU_113664_3_2_6; -.
DR   OMA; TPWYQFF; -.
DR   Proteomes; UP000000642; 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; Stress response.
FT   CHAIN           1..157
FT                   /note="DNA gyrase inhibitor"
FT                   /id="PRO_0000409708"
SQ   SEQUENCE   157 AA;  17989 MW;  853F355853036DF4 CRC64;
     MAFKIIEKQP QQIVSIRVVG PYHETIPKGF DQLSSLYTQY QIPGKDWLVL YWDNPETNPP
     AELRADVSLS VADDYVLPPE LSDHLQLQVI PAGLYAVYHT RVSDDDYAKA WGELYNQHLP
     QSGYRPTEGA CYEVYLNDGR ADGYFDIDIY QSVEKDQ