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SBMC_SERP5
ID   SBMC_SERP5              Reviewed;         156 AA.
AC   A8GG82;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=DNA gyrase inhibitor {ECO:0000255|HAMAP-Rule:MF_01896};
GN   Name=sbmC {ECO:0000255|HAMAP-Rule:MF_01896}; OrderedLocusNames=Spro_3021;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-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}.
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DR   EMBL; CP000826; ABV42122.1; -; Genomic_DNA.
DR   RefSeq; WP_012145743.1; NC_009832.1.
DR   AlphaFoldDB; A8GG82; -.
DR   SMR; A8GG82; -.
DR   STRING; 399741.Spro_3021; -.
DR   EnsemblBacteria; ABV42122; ABV42122; Spro_3021.
DR   KEGG; spe:Spro_3021; -.
DR   eggNOG; COG3449; Bacteria.
DR   HOGENOM; CLU_113664_3_0_6; -.
DR   OMA; TPWYQFF; -.
DR   OrthoDB; 1748122at2; -.
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..156
FT                   /note="DNA gyrase inhibitor"
FT                   /id="PRO_0000409706"
SQ   SEQUENCE   156 AA;  17697 MW;  37727F62D525046A CRC64;
     MTVRIEDKSA ERVVGVRVVG PYPQTIPQGC QRLMAWQQQH QVPLGKWLVL YWDDPAEVAP
     ERLRADVVFT VADDFVLPTS GSEGFALQTL PAGQYAIYNV RVSDGDFERV WGDFYQRELP
     ASGYQPVEGV SYEHYLNDCE ADGYFDLDIY QTVKKG
 
 
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