ID   HAT_MYCTU               Reviewed;          76 AA.
AC   P9WKY5; Q8VJ11;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=Histone acetyltransferase {ECO:0000303|PubMed:26476134};
DE            Short=HAT {ECO:0000303|PubMed:26476134};
DE            EC=2.3.1.48 {ECO:0000269|PubMed:26476134};
GN   OrderedLocusNames=Rv3423.1;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-12, AND MASS SPECTROMETRY.
RC   STRAIN=ATCC 25618 / H37Rv;
RA   Jose L., Lakshmanan D., Mundayoor S., Kumar R.A.;
RL   Submitted (MAY-2008) to UniProtKB.
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY,
RP   SUBCELLULAR LOCATION, 3D-STRUCTURE MODELING, ACTIVITY REGULATION,
RP   INDUCTION, AND INTERACTION WITH HISTONE H3.
RC   STRAIN=H37Rv;
RX   PubMed=26476134; DOI=10.1111/febs.13566;
RA   Jose L., Ramachandran R., Bhagavat R., Gomez R.L., Chandran A.,
RA   Raghunandanan S., Omkumar R.V., Chandra N., Mundayoor S., Kumar R.A.;
RT   "Hypothetical protein Rv3423.1 of Mycobacterium tuberculosis is a histone
RT   acetyltransferase.";
RL   FEBS J. 283:265-281(2016).
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:0000269|PubMed:26476134}.
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:0000269|PubMed:26476134};
CC   -!- ACTIVITY REGULATION: Is completely inhibited by anacardic acid, an
CC       inhibitor of HAT activity. {ECO:0000269|PubMed:26476134}.
CC   -!- SUBUNIT: Physically interacts with histone H3 in infected macrophages.
CC       {ECO:0000269|PubMed:26476134}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26476134}. Host
CC       cytoplasm {ECO:0000269|PubMed:26476134}. Host nucleus
CC       {ECO:0000269|PubMed:26476134}. Note=Colocalizes with the chromatin in
CC       the nucleus of infected human macrophages.
CC       {ECO:0000269|PubMed:26476134}.
CC   -!- INDUCTION: Expression of this gene marginally increases (1.5-fold) in
CC       macrophages from 12 to 24 hours post-infection, and does not decrease
CC       up to 60 h. {ECO:0000269|PubMed:26476134}.
CC   -!- MASS SPECTROMETRY: Mass=8436.1; Method=MALDI;
CC       Evidence={ECO:0000269|Ref.2};
CC   -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is:
CC       9.47.
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DR   EMBL; AL123456; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; WP_003900685.1; NZ_NVQJ01000027.1.
DR   AlphaFoldDB; P9WKY5; -.
DR   TubercuList; Rv3423.1; -.
DR   Proteomes; UP000001584; 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; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR   GO; GO:0010484; F:H3 histone acetyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR   GO; GO:0016573; P:histone acetylation; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Acyltransferase; Direct protein sequencing; Host cytoplasm; Host nucleus;
KW   Reference proteome; Secreted; Transferase.
FT   CHAIN           1..76
FT                   /note="Histone acetyltransferase"
FT                   /id="PRO_0000343615"
SQ   SEQUENCE   76 AA;  8442 MW;  F84EFAEB55CBE8E6 CRC64;
     MSFGFPTFSQ NRFTEQYSGL CPIAPGRGAG LQPCRRDCPV ARWLVADHPV FGSDCRCRMM
     VGVNRVRIGR HELTGA