ID   ECTA_BORPA              Reviewed;         186 AA.
AC   Q7W980;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=L-2,4-diaminobutyric acid acetyltransferase;
DE            Short=DABA acetyltransferase;
DE            EC=2.3.1.178;
GN   Name=ectA; OrderedLocusNames=BPP1888;
OS   Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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}.
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DR   EMBL; BX640428; CAE37189.1; -; Genomic_DNA.
DR   RefSeq; WP_010928263.1; NC_002928.3.
DR   PDB; 3D3S; X-ray; 1.87 A; A/B/C/D=1-186.
DR   PDBsum; 3D3S; -.
DR   AlphaFoldDB; Q7W980; -.
DR   SMR; Q7W980; -.
DR   EnsemblBacteria; CAE37189; CAE37189; BPP1888.
DR   KEGG; bpa:BPP1888; -.
DR   HOGENOM; CLU_111896_0_0_4; -.
DR   OMA; DGAAIWR; -.
DR   UniPathway; UPA00067; UER00122.
DR   EvolutionaryTrace; Q7W980; -.
DR   Proteomes; UP000001421; 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   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Transferase.
FT   CHAIN           1..186
FT                   /note="L-2,4-diaminobutyric acid acetyltransferase"
FT                   /id="PRO_0000220084"
FT   DOMAIN          24..179
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   STRAND          25..27
FT                   /evidence="ECO:0007829|PDB:3D3S"
FT   HELIX           31..33
FT                   /evidence="ECO:0007829|PDB:3D3S"
FT   HELIX           34..42
FT                   /evidence="ECO:0007829|PDB:3D3S"
FT   HELIX           52..61
FT                   /evidence="ECO:0007829|PDB:3D3S"
FT   HELIX           63..65
FT                   /evidence="ECO:0007829|PDB:3D3S"
FT   STRAND          67..70
FT                   /evidence="ECO:0007829|PDB:3D3S"
FT   STRAND          76..84
FT                   /evidence="ECO:0007829|PDB:3D3S"
FT   STRAND          91..99
FT                   /evidence="ECO:0007829|PDB:3D3S"
FT   HELIX           101..103
FT                   /evidence="ECO:0007829|PDB:3D3S"
FT   HELIX           108..118
FT                   /evidence="ECO:0007829|PDB:3D3S"
FT   HELIX           120..122
FT                   /evidence="ECO:0007829|PDB:3D3S"
FT   STRAND          127..132
FT                   /evidence="ECO:0007829|PDB:3D3S"
FT   HELIX           137..148
FT                   /evidence="ECO:0007829|PDB:3D3S"
FT   TURN            149..151
FT                   /evidence="ECO:0007829|PDB:3D3S"
FT   STRAND          153..160
FT                   /evidence="ECO:0007829|PDB:3D3S"
FT   HELIX           162..165
FT                   /evidence="ECO:0007829|PDB:3D3S"
FT   STRAND          173..179
FT                   /evidence="ECO:0007829|PDB:3D3S"
SQ   SEQUENCE   186 AA;  20729 MW;  C0B7C716917F9CF4 CRC64;
     MRKDETSNTS PDISVAQPAS ALRYHLRPPR RNDGAAIHQL VSECPPLDLN SLYAYLLLCE
     HHAHTCVVAE SPGGRIDGFV SAYLLPTRPD VLFVWQVAVH SRARGHRLGR AMLGHILERQ
     ECRHVRHLET TVGPDNQASR RTFAGLAGER GAHVSEQPFF DRQAFGGADH DDEMLLRIGP
     FTHPPH