ID   HAT_MYCTO               Reviewed;          76 AA.
AC   P9WKY4; Q8VJ11;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Histone acetyltransferase {ECO:0000250|UniProtKB:P9WKY5};
DE            Short=HAT {ECO:0000250|UniProtKB:P9WKY5};
DE            EC=2.3.1.48 {ECO:0000250|UniProtKB:P9WKY5};
GN   OrderedLocusNames=MT3532.1;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Histone acetyltransferase, which by binding to the host
CC       chromatin, may manipulate the expression of host genes involved in
CC       anti-inflammatory responses to evade clearance and to survive in the
CC       intracellular milieu. Acetylates histone H3 at the 'Lys-9' and 'Lys-14'
CC       positions. {ECO:0000250|UniProtKB:P9WKY5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC         lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC         Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC         Evidence={ECO:0000250|UniProtKB:P9WKY5};
CC   -!- ACTIVITY REGULATION: Is completely inhibited by anacardic acid, an
CC       inhibitor of HAT activity. {ECO:0000250|UniProtKB:P9WKY5}.
CC   -!- SUBUNIT: Physically interacts with histone H3 in infected macrophages.
CC       {ECO:0000250|UniProtKB:P9WKY5}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P9WKY5}. Host
CC       cytoplasm {ECO:0000250|UniProtKB:P9WKY5}. Host nucleus
CC       {ECO:0000250|UniProtKB:P9WKY5}. Note=Colocalizes with the chromatin in
CC       the nucleus of infected human macrophages.
CC       {ECO:0000250|UniProtKB:P9WKY5}.
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DR   EMBL; AE000516; AAK47871.1; -; Genomic_DNA.
DR   RefSeq; WP_003900685.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WKY4; -.
DR   EnsemblBacteria; AAK47871; AAK47871; MT3532.1.
DR   KEGG; mtc:MT3532.1; -.
DR   HOGENOM; CLU_2650630_0_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
PE   3: Inferred from homology;
KW   Acyltransferase; Host cytoplasm; Host nucleus; Secreted; Transferase.
FT   CHAIN           1..76
FT                   /note="Histone acetyltransferase"
FT                   /id="PRO_0000427573"
SQ   SEQUENCE   76 AA;  8442 MW;  F84EFAEB55CBE8E6 CRC64;
     MSFGFPTFSQ NRFTEQYSGL CPIAPGRGAG LQPCRRDCPV ARWLVADHPV FGSDCRCRMM
     VGVNRVRIGR HELTGA