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YACG_NEIMB
ID   YACG_NEIMB              Reviewed;          69 AA.
AC   Q9K155;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=DNA gyrase inhibitor YacG {ECO:0000255|HAMAP-Rule:MF_00649};
GN   Name=yacG {ECO:0000255|HAMAP-Rule:MF_00649}; OrderedLocusNames=NMB0330;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
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; AE002098; AAF40774.1; -; Genomic_DNA.
DR   PIR; F81210; F81210.
DR   RefSeq; NP_273379.1; NC_003112.2.
DR   RefSeq; WP_002224872.1; NC_003112.2.
DR   AlphaFoldDB; Q9K155; -.
DR   SMR; Q9K155; -.
DR   STRING; 122586.NMB0330; -.
DR   PaxDb; Q9K155; -.
DR   EnsemblBacteria; AAF40774; AAF40774; NMB0330.
DR   KEGG; nme:NMB0330; -.
DR   PATRIC; fig|122586.8.peg.418; -.
DR   HOGENOM; CLU_178280_3_2_4; -.
DR   OMA; WAAEEHK; -.
DR   Proteomes; UP000000425; 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..69
FT                   /note="DNA gyrase inhibitor YacG"
FT                   /id="PRO_0000211711"
FT   BINDING         13
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00649"
FT   BINDING         16
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"
FT   BINDING         36
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00649"
SQ   SEQUENCE   69 AA;  7841 MW;  2402316DAAA77096 CRC64;
     MTESRQTRLQ VKCPTCQTAV VWKPENAFRP FCSQRCKLID LGGWADGKYT VSGQTESLPE
     ISEPDMAYR
 
 
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