ID   SBMC_ENTLS              Reviewed;         157 AA.
AC   E3G128;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=DNA gyrase inhibitor {ECO:0000255|HAMAP-Rule:MF_01896};
GN   Name=sbmC {ECO:0000255|HAMAP-Rule:MF_01896}; OrderedLocusNames=Entcl_1682;
OS   Enterobacter lignolyticus (strain SCF1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Pluralibacter.
OX   NCBI_TaxID=701347;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCF1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA   Mikhailova N., DeAngelis K., Arkin A.P., Chivian D., Edwards B., Woo H.,
RA   Hazen T.C., Woyke T.;
RT   "Complete sequence of Enterobacter cloacae SCF1.";
RL   Submitted (OCT-2010) 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}.
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DR   EMBL; CP002272; ADO47942.1; -; Genomic_DNA.
DR   RefSeq; WP_013365686.1; NC_014618.1.
DR   AlphaFoldDB; E3G128; -.
DR   SMR; E3G128; -.
DR   STRING; 701347.Entcl_1682; -.
DR   EnsemblBacteria; ADO47942; ADO47942; Entcl_1682.
DR   KEGG; esc:Entcl_1682; -.
DR   eggNOG; COG3449; Bacteria.
DR   HOGENOM; CLU_113664_3_2_6; -.
DR   OMA; TPWYQFF; -.
DR   OrthoDB; 1748122at2; -.
DR   Proteomes; UP000006872; 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_0000409697"
SQ   SEQUENCE   157 AA;  17900 MW;  5151DEC41F47B2D3 CRC64;
     MEYSIRQEQQ RVVAGFHMVG PWEQTVKQGF EQLMMWVDGR DIPAKEWLAV YYDNPDEVPA
     EKLRCDTVVT VEPGFQIPAN SEGVMLTQVS GGEYAVASAR VVNHDFATPW YQFFGSVLAD
     TAWEMAAKPC FERYLNDGNQ DGYWDIEMYI AVSRRAG