ID   SBMC_KLEP3              Reviewed;         157 AA.
AC   B5XPH8;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 57.
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=KPK_1720;
OS   Klebsiella pneumoniae (strain 342).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=507522;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342;
RX   PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA   Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA   Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA   Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA   Methe B.A.;
RT   "Complete genome sequence of the N2-fixing broad host range endophyte
RT   Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL   PLoS Genet. 4:E1000141-E1000141(2008).
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; CP000964; ACI07477.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5XPH8; -.
DR   SMR; B5XPH8; -.
DR   EnsemblBacteria; ACI07477; ACI07477; KPK_1720.
DR   KEGG; kpe:KPK_1720; -.
DR   HOGENOM; CLU_113664_3_2_6; -.
DR   OMA; TPWYQFF; -.
DR   OrthoDB; 1748122at2; -.
DR   Proteomes; UP000001734; 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_0000409702"
SQ   SEQUENCE   157 AA;  17775 MW;  9001EE611FB7933D CRC64;
     MNYSITTLGK KTIAGFHLVG PWDQTVKQGV EQLMMWVENH QVPAREWLAV YYDNPEEVPA
     EKLRCATVVA VDEDYVIPAN SEGVILAAVA GGDYACARAR VVDYDFATPW MQFFDSLLQS
     TTYRVAPRPC FEIYLNDGNH DGYWDIDMYV PVERVAS