ID   ECTA_SPOPA              Reviewed;         180 AA.
AC   Q9AP35;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=L-2,4-diaminobutyric acid acetyltransferase;
DE            Short=DABA acetyltransferase;
DE            EC=2.3.1.178;
GN   Name=ectA;
OS   Sporosarcina pasteurii (Bacillus pasteurii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX   NCBI_TaxID=1474;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TRANSCRIPTIONAL REGULATION.
RC   STRAIN=ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822;
RX   PubMed=11823218; DOI=10.1128/aem.68.2.772-783.2002;
RA   Kuhlmann A.U., Bremer E.;
RT   "Osmotically regulated synthesis of the compatible solute ectoine in
RT   Bacillus pasteurii and related Bacillus spp.";
RL   Appl. Environ. Microbiol. 68:772-783(2002).
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:0000305}.
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   -!- INDUCTION: By osmotic stress. {ECO:0000269|PubMed:11823218}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. EctA subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF316874; AAK12083.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9AP35; -.
DR   SMR; Q9AP35; -.
DR   KEGG; ag:AAK12083; -.
DR   UniPathway; UPA00067; UER00122.
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   2: Evidence at transcript level;
KW   Acyltransferase; Stress response; Transferase.
FT   CHAIN           1..180
FT                   /note="L-2,4-diaminobutyric acid acetyltransferase"
FT                   /id="PRO_0000220081"
FT   DOMAIN          20..180
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   180 AA;  20717 MW;  74F512D80C679892 CRC64;
     MFWVISKQGS TAVAEQEETL VFRVPTEDDG KAIWNLINYP GVLDLLSSYS YFMWAKFFDQ
     TSVVGETNEQ IVGFYIGLHT TEYGPDTLFY LASCSDETQR QKGLASRMLQ AILHRYAWRN
     IRYLEATVGT SNEAPEALFQ KLSRDLKTAY HVTEFFTEDQ FPGKGHEDER LFKIGPFQQV