YACG_SALPA
ID YACG_SALPA Reviewed; 63 AA.
AC Q5PDD8;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=DNA gyrase inhibitor YacG {ECO:0000255|HAMAP-Rule:MF_00649};
GN Name=yacG {ECO:0000255|HAMAP-Rule:MF_00649}; OrderedLocusNames=SPA0142;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV76175.1; -; Genomic_DNA.
DR RefSeq; WP_001286418.1; NC_006511.1.
DR AlphaFoldDB; Q5PDD8; -.
DR SMR; Q5PDD8; -.
DR EnsemblBacteria; AAV76175; AAV76175; SPA0142.
DR KEGG; spt:SPA0142; -.
DR HOGENOM; CLU_178280_3_1_6; -.
DR OMA; WAAEEHK; -.
DR Proteomes; UP000008185; 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; Zinc.
FT CHAIN 1..63
FT /note="DNA gyrase inhibitor YacG"
FT /id="PRO_0000211722"
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 63 AA; 7019 MW; 739EC6248683FB5A CRC64;
MSDVTVVNCP TCGKPVVWGE ISPFRPFCSK RCQLIDLGEW AAEEKRIASS GDPSDSDDWS
EER
