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Database: UniProt
Entry: F7VCG0_9PROT
LinkDB: F7VCG0_9PROT
Original site: F7VCG0_9PROT 
ID   F7VCG0_9PROT            Unreviewed;       336 AA.
AC   F7VCG0;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=N-alpha-acetyl diaminobutyric acid deacetylase DoeB {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ATPR_1059 {ECO:0000313|EMBL:GAA08055.1};
OS   Acetobacter tropicalis NBRC 101654.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter.
OX   NCBI_TaxID=749388 {ECO:0000313|EMBL:GAA08055.1, ECO:0000313|Proteomes:UP000004319};
RN   [1] {ECO:0000313|EMBL:GAA08055.1, ECO:0000313|Proteomes:UP000004319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101654 {ECO:0000313|EMBL:GAA08055.1,
RC   ECO:0000313|Proteomes:UP000004319};
RX   PubMed=21554859; DOI=10.1016/j.bbrc.2011.04.126;
RA   Matsutani M., Hirakawa H., Nishikura M., Soemphol W., Ali I.A.I.,
RA   Yakushi T., Matsushita K.;
RT   "Increased number of Arginine-based salt bridges contributes to the
RT   thermotolerance of thermotolerant acetic acid bacteria, Acetobacter
RT   tropicalis SKU1100.";
RL   Biochem. Biophys. Res. Commun. 409:120-124(2011).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAA08055.1}.
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DR   EMBL; BABS01000021; GAA08055.1; -; Genomic_DNA.
DR   RefSeq; WP_006558074.1; NZ_BABS01000021.1.
DR   AlphaFoldDB; F7VCG0; -.
DR   Proteomes; UP000004319; Unassembled WGS sequence.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd06252; M14_ASTE_ASPA-like; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR007036; Aste_AspA.
DR   InterPro; IPR014336; DoeB.
DR   InterPro; IPR043795; N-alpha-Ac-DABA-like.
DR   NCBIfam; TIGR02994; ectoine_eutE; 1.
DR   PANTHER; PTHR37326; BLL3975 PROTEIN; 1.
DR   PANTHER; PTHR37326:SF1; BLL3975 PROTEIN; 1.
DR   Pfam; PF04952; AstE_AspA; 1.
DR   PIRSF; PIRSF039012; ASP; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ   SEQUENCE   336 AA;  36258 MW;  35DFCE01BCE52F1B CRC64;
     MTDTQLDSPI VATVPFDKDG IHHGFLRLPY SRDDSAWGSI MIPLTVVRNG EGPTALLTGG
     NHGDEYEGPV ALFGLAQELD PLDVSGCVII VPAMNYPAFR AATRTSPIDR GNMNRIFPGR
     PDGTVTEKIA DYFQRVLLPM CDIVLDFHSG GKTLDFIPFA AAHVLPDPVQ EEKCFSAVKA
     FGAPYSLKMV EIDSRGMFDT AIEEMGKVFV TTELGGGGTV SARTAEIARQ GVRNVLRHMG
     ILAGEVVTSP TQWLDMPGDE SFVFAAQDGL LEMCVDLEAP VKKGQTIARI HTIDRTGVEP
     TRILAPCDGI LIARHFPGLI KMGDCVASFG VVIEDL
//
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