(data stored in SCRATCH zone)

SWISSPROT: C8U1H2_ECO10

ID   C8U1H2_ECO10            Unreviewed;        65 AA.
AC   C8U1H2;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 58.
DE   RecName: Full=DNA gyrase inhibitor YacG {ECO:0000256|HAMAP-Rule:MF_00649, ECO:0000256|SAAS:SAAS00382377};
GN   Name=yacG {ECO:0000256|HAMAP-Rule:MF_00649,
GN   ECO:0000313|EMBL:BAI28980.1};
GN   OrderedLocusNames=ECO103_0102 {ECO:0000313|EMBL:BAI28980.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI28980.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI28980.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Inhibits all the catalytic activities of DNA gyrase by
CC       preventing its interaction with DNA. Acts by binding directly to
CC       the C-terminal domain of GyrB, which probably disrupts DNA binding
CC       by the gyrase. {ECO:0000256|HAMAP-Rule:MF_00649,
CC       ECO:0000256|SAAS:SAAS00085449}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00649};
CC       Note=Binds 1 zinc ion. {ECO:0000256|HAMAP-Rule:MF_00649};
CC   -!- SUBUNIT: Interacts with GyrB. {ECO:0000256|HAMAP-Rule:MF_00649,
CC       ECO:0000256|SAAS:SAAS00085444}.
CC   -!- SIMILARITY: Belongs to the DNA gyrase inhibitor YacG family.
CC       {ECO:0000256|HAMAP-Rule:MF_00649, ECO:0000256|SAAS:SAAS00570156}.
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DR   EMBL; AP010958; BAI28980.1; -; Genomic_DNA.
DR   RefSeq; WP_000005042.1; NC_013353.1.
DR   SMR; C8U1H2; -.
DR   EnsemblBacteria; BAI28980; BAI28980; ECO103_0102.
DR   KEGG; eoh:ECO103_0102; -.
DR   HOGENOM; HOG000255917; -.
DR   KO; K09862; -.
DR   OMA; FRPFCSD; -.
DR   BioCyc; ECOL585395:ECO103_RS00520-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0008657; F:DNA topoisomerase (ATP-hydrolyzing) inhibitor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 3.30.50.10; -; 1.
DR   HAMAP; MF_00649; DNA_gyrase_inhibitor_YacG; 1.
DR   InterPro; IPR005584; DNA_gyrase_inhibitor_YacG.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   PANTHER; PTHR36150; PTHR36150; 1.
DR   Pfam; PF03884; YacG; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U1H2.
DR   SWISS-2DPAGE; C8U1H2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00649,
KW   ECO:0000256|SAAS:SAAS00459510};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00649, ECO:0000256|SAAS:SAAS00459506}.
FT   METAL         9      9       Zinc. {ECO:0000256|HAMAP-Rule:MF_00649}.
FT   METAL        12     12       Zinc. {ECO:0000256|HAMAP-Rule:MF_00649}.
FT   METAL        28     28       Zinc. {ECO:0000256|HAMAP-Rule:MF_00649}.
FT   METAL        32     32       Zinc. {ECO:0000256|HAMAP-Rule:MF_00649}.
SQ   SEQUENCE   65 AA;  7306 MW;  F2747B62AFE6479D CRC64;
     MSETITVNCP TCGKTVVWGE ISPFRPFCSK RCQLIDLGEW AAEEKRIPSS GDLSESDDWS
     EEPKQ
//

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