YACG_HYPNA
ID YACG_HYPNA Reviewed; 73 AA.
AC Q0C1F7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=DNA gyrase inhibitor YacG {ECO:0000255|HAMAP-Rule:MF_00649};
GN Name=yacG {ECO:0000255|HAMAP-Rule:MF_00649}; OrderedLocusNames=HNE_1731;
OS Hyphomonas neptunium (strain ATCC 15444).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomonadales;
OC Hyphomonadaceae; Hyphomonas.
OX NCBI_TaxID=228405;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15444;
RX PubMed=16980487; DOI=10.1128/jb.00111-06;
RA Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., Alexandre G.,
RA Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., Khouri H.M., Radune D.,
RA Sosa J., Dodson R.J., Sullivan S.A., Rosovitz M.J., Madupu R.,
RA Brinkac L.M., Durkin A.S., Daugherty S.C., Kothari S.P., Giglio M.G.,
RA Zhou L., Haft D.H., Selengut J.D., Davidsen T.M., Yang Q., Zafar N.,
RA Ward N.L.;
RT "Comparative genomic evidence for a close relationship between the
RT dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter
RT crescentus.";
RL J. Bacteriol. 188:6841-6850(2006).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000158; ABI78222.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0C1F7; -.
DR SMR; Q0C1F7; -.
DR STRING; 228405.HNE_1731; -.
DR PRIDE; Q0C1F7; -.
DR EnsemblBacteria; ABI78222; ABI78222; HNE_1731.
DR KEGG; hne:HNE_1731; -.
DR eggNOG; COG3024; Bacteria.
DR HOGENOM; CLU_178280_2_0_5; -.
DR OMA; FHPFCSK; -.
DR OrthoDB; 2071775at2; -.
DR Proteomes; UP000001959; 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 Pfam; PF03884; YacG; 1.
PE 3: Inferred from homology;
KW Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..73
FT /note="DNA gyrase inhibitor YacG"
FT /id="PRO_1000056977"
FT REGION 54..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00649"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00649"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00649"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00649"
SQ SEQUENCE 73 AA; 7723 MW; DD99203E1F4D3279 CRC64;
MSKPVNPSQR TPLCARCRKQ AVAAEYRPFC SKRCADADLG QWLKGGYVIP GAAAEQADDT
AGPGAAEDDT DSH
