SBMC_CITK8
ID SBMC_CITK8 Reviewed; 155 AA.
AC A8AEL4;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=DNA gyrase inhibitor {ECO:0000255|HAMAP-Rule:MF_01896};
GN Name=sbmC {ECO:0000255|HAMAP-Rule:MF_01896}; OrderedLocusNames=CKO_00775;
OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=290338;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG The Citrobacter koseri Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000822; ABV11927.1; -; Genomic_DNA.
DR RefSeq; WP_012131750.1; NC_009792.1.
DR AlphaFoldDB; A8AEL4; -.
DR SMR; A8AEL4; -.
DR STRING; 290338.CKO_00775; -.
DR EnsemblBacteria; ABV11927; ABV11927; CKO_00775.
DR GeneID; 45134974; -.
DR KEGG; cko:CKO_00775; -.
DR HOGENOM; CLU_113664_3_2_6; -.
DR OMA; TPWYQFF; -.
DR OrthoDB; 1748122at2; -.
DR Proteomes; UP000008148; 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_0000409690"
SQ SEQUENCE 155 AA; 17876 MW; 58426A2B9129F1CB CRC64;
MDYEIRQAEK RNIAGFHMVG PWEKTVKQGF EQLMMWVDGN QVVPLEWIAV YYDNPDEVPA
EKLRCDTVVS VPDNFTIPKN SEGVILTEIA GGQYATAVAR VENHDFATPW YQFFNSLLQD
NHYQIAAKPC FEVYLNNGTE DGYWDIEMYV PVQSK