SBMC_ERWBE
ID SBMC_ERWBE Reviewed; 155 AA.
AC D8MUB2;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, 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}; OrderedLocusNames=EbC_28880;
OS Erwinia billingiae (strain Eb661).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=634500;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eb661;
RX PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA Knaust F., Geider K., Reinhardt R.;
RT "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT tasmaniensis with the pear pathogen E. pyrifoliae.";
RL BMC Genomics 11:393-393(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; FP236843; CAX60419.1; -; Genomic_DNA.
DR RefSeq; WP_013202904.1; NC_014306.1.
DR AlphaFoldDB; D8MUB2; -.
DR SMR; D8MUB2; -.
DR STRING; 634500.EbC_28880; -.
DR EnsemblBacteria; CAX60419; CAX60419; EbC_28880.
DR KEGG; ebi:EbC_28880; -.
DR eggNOG; COG3449; Bacteria.
DR HOGENOM; CLU_113664_3_2_6; -.
DR OMA; TPWYQFF; -.
DR OrthoDB; 1748122at2; -.
DR Proteomes; UP000008793; 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_0000409700"
SQ SEQUENCE 155 AA; 17276 MW; 3CB656C2A8EDD88D CRC64;
MNVEIVEREE SKTAGFHLVG PWEVTAPEGF DKLVAWTSKH NVMGPWMGVY HGNPRAVPAE
ELKIETVIGV PTDFELPEGS EGARLSIIPA GTYAMNLVHV NDGDFTKPWY AFFDEWLPDS
GYVMAEGPCF DHYLNDGSQS GEWDIELYIP VSKAE