ID   ECTA_ALKCK              Reviewed;         178 AA.
AC   Q5WL79;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=L-2,4-diaminobutyric acid acetyltransferase;
DE            Short=DABA acetyltransferase;
DE            EC=2.3.1.178;
GN   Name=ectA; OrderedLocusNames=ABC0334;
OS   Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=66692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16;
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT   K16.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the acetylation of L-2,4-diaminobutyrate (DABA) to
CC       gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) with acetyl
CC       coenzyme A. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-2,4-diaminobutanoate = (2S)-4-acetamido-2-
CC         aminobutanoate + CoA + H(+); Xref=Rhea:RHEA:16901, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58761,
CC         ChEBI:CHEBI:58929; EC=2.3.1.178;
CC   -!- PATHWAY: Amine and polyamine biosynthesis; ectoine biosynthesis; L-
CC       ectoine from L-aspartate 4-semialdehyde: step 2/3.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. EctA subfamily.
CC       {ECO:0000305}.
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; AP006627; BAD62876.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5WL79; -.
DR   SMR; Q5WL79; -.
DR   STRING; 66692.ABC0334; -.
DR   EnsemblBacteria; BAD62876; BAD62876; ABC0334.
DR   KEGG; bcl:ABC0334; -.
DR   eggNOG; COG0456; Bacteria.
DR   HOGENOM; CLU_111896_0_0_9; -.
DR   OMA; DGAAIWR; -.
DR   UniPathway; UPA00067; UER00122.
DR   Proteomes; UP000001168; Chromosome.
DR   GO; GO:0033816; F:diaminobutyrate acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR   GO; GO:0019491; P:ectoine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR012772; Ectoine_EctA.
DR   InterPro; IPR000182; GNAT_dom.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   TIGRFAMs; TIGR02406; ectoine_EctA; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..178
FT                   /note="L-2,4-diaminobutyric acid acetyltransferase"
FT                   /id="PRO_0000220082"
FT   DOMAIN          21..174
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   178 AA;  19849 MW;  F7010104657536DC CRC64;
     MSGKNEIINE KEAVMVQTPV LTLTKPTVED GAAMWQLAKS SSLDTNSSYK YIMMCEYFDD
     TCIVAKDGDE VVGFITAFIP PKQQDTLFIW QIGVAASQRG RGLGLDLINK LIEREACKDI
     RYVEATVTPS NKASQALFRK LARSHQTDCQ VSSCFSEQLF PGDSHEQENT FRIGPLRS