ID   SBMC_CITRI              Reviewed;         157 AA.
AC   D2TPS8;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=DNA gyrase inhibitor {ECO:0000255|HAMAP-Rule:MF_01896};
GN   Name=sbmC {ECO:0000255|HAMAP-Rule:MF_01896}; OrderedLocusNames=ROD_21481;
OS   Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=637910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICC168;
RX   PubMed=19897651; DOI=10.1128/jb.01144-09;
RA   Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N.,
RA   Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L.,
RA   Parkhill J., Dougan G., Frankel G., Thomson N.R.;
RT   "The Citrobacter rodentium genome sequence reveals convergent evolution
RT   with human pathogenic Escherichia coli.";
RL   J. Bacteriol. 192:525-538(2010).
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; FN543502; CBG88896.1; -; Genomic_DNA.
DR   RefSeq; WP_012906351.1; NC_013716.1.
DR   AlphaFoldDB; D2TPS8; -.
DR   SMR; D2TPS8; -.
DR   STRING; 637910.ROD_21481; -.
DR   KEGG; cro:ROD_21481; -.
DR   eggNOG; COG3449; Bacteria.
DR   HOGENOM; CLU_113664_3_2_6; -.
DR   OMA; TPWYQFF; -.
DR   OrthoDB; 1748122at2; -.
DR   Proteomes; UP000001889; 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..157
FT                   /note="DNA gyrase inhibitor"
FT                   /id="PRO_0000409691"
SQ   SEQUENCE   157 AA;  17912 MW;  20A0F59AD930B01C CRC64;
     MNYEIRQVDK RTVAGFHLVG PWEQTVKQGF EQLMKWVEGR QIVTDEWIAV YFDNPDVVPA
     EKLRCSTVVS VPADFVVPAN SEGVSLSEID GGQYATAVAR VTDNDFSTPW YQFFNSLAQD
     NKYEMACKPC FEVYLNDGCT EGYWDIEMYI AVQPLSR