YACG_PROMH
ID YACG_PROMH Reviewed; 71 AA.
AC B4F0Z6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=DNA gyrase inhibitor YacG {ECO:0000255|HAMAP-Rule:MF_00649};
GN Name=yacG {ECO:0000255|HAMAP-Rule:MF_00649}; OrderedLocusNames=PMI2054;
OS Proteus mirabilis (strain HI4320).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=529507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI4320;
RX PubMed=18375554; DOI=10.1128/jb.01981-07;
RA Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA Parkhill J., Mobley H.L.T.;
RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT both adherence and motility.";
RL J. Bacteriol. 190:4027-4037(2008).
CC -!- FUNCTION: Inhibits all the catalytic activities of DNA gyrase by
CC preventing its interaction with DNA. Acts by binding directly to the C-
CC terminal domain of GyrB, which probably disrupts DNA binding by the
CC gyrase. {ECO:0000255|HAMAP-Rule:MF_00649}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00649};
CC Note=Binds 1 zinc ion. {ECO:0000255|HAMAP-Rule:MF_00649};
CC -!- SUBUNIT: Interacts with GyrB. {ECO:0000255|HAMAP-Rule:MF_00649}.
CC -!- SIMILARITY: Belongs to the DNA gyrase inhibitor YacG family.
CC {ECO:0000255|HAMAP-Rule:MF_00649}.
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DR EMBL; AM942759; CAR44115.1; -; Genomic_DNA.
DR RefSeq; WP_004244091.1; NC_010554.1.
DR AlphaFoldDB; B4F0Z6; -.
DR SMR; B4F0Z6; -.
DR STRING; 529507.PMI2054; -.
DR EnsemblBacteria; CAR44115; CAR44115; PMI2054.
DR GeneID; 6802895; -.
DR KEGG; pmr:PMI2054; -.
DR eggNOG; COG3024; Bacteria.
DR HOGENOM; CLU_178280_3_1_6; -.
DR OMA; WAAEEHK; -.
DR Proteomes; UP000008319; Chromosome.
DR GO; GO:0008657; F:DNA topoisomerase type II (double strand cut, 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;
KW Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..71
FT /note="DNA gyrase inhibitor YacG"
FT /id="PRO_1000130967"
FT REGION 43..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00649"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00649"
FT BINDING 28
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00649"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00649"
SQ SEQUENCE 71 AA; 8325 MW; 609995DDEB006BCD CRC64;
MSEKLIVKCP TCRTEVIWDE SSPYRPFCCK RCQLIDLGEW AAEEKRIPSQ SESNDSDEWS
EMPEQDPKPF N