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Database: UniProt
Entry: A0A120AH56_9GAMM
LinkDB: A0A120AH56_9GAMM
Original site: A0A120AH56_9GAMM 
ID   A0A120AH56_9GAMM        Unreviewed;       472 AA.
AC   A0A120AH56;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:KWS05648.1};
DE            EC=3.4.16.4 {ECO:0000313|EMBL:KWS05648.1};
GN   ORFNames=AZ78_3200 {ECO:0000313|EMBL:KWS05648.1};
OS   Lysobacter capsici AZ78.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=1444315 {ECO:0000313|EMBL:KWS05648.1, ECO:0000313|Proteomes:UP000023435};
RN   [1] {ECO:0000313|EMBL:KWS05648.1, ECO:0000313|Proteomes:UP000023435}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AZ78 {ECO:0000313|EMBL:KWS05648.1,
RC   ECO:0000313|Proteomes:UP000023435};
RX   PubMed=24762937;
RA   Puopolo G., Sonego P., Engelen K., Pertot I.;
RT   "Draft Genome Sequence of Lysobacter capsici AZ78, a Bacterium Antagonistic
RT   to Plant-Pathogenic Oomycetes.";
RL   Genome Announc. 2:0-0(2014).
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:KWS05648.1}.
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DR   EMBL; JAJA02000001; KWS05648.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A120AH56; -.
DR   Proteomes; UP000023435; Unassembled WGS sequence.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR001466; Beta-lactam-related.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   PANTHER; PTHR46825; D-ALANYL-D-ALANINE-CARBOXYPEPTIDASE/ENDOPEPTIDASE AMPH; 1.
DR   PANTHER; PTHR46825:SF9; PROTEIN FLP; 1.
DR   Pfam; PF00144; Beta-lactamase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:KWS05648.1};
KW   Hydrolase {ECO:0000313|EMBL:KWS05648.1};
KW   Protease {ECO:0000313|EMBL:KWS05648.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..472
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007163680"
FT   DOMAIN          45..346
FT                   /note="Beta-lactamase-related"
FT                   /evidence="ECO:0000259|Pfam:PF00144"
FT   REGION          453..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   472 AA;  50694 MW;  43953E69360310E6 CRC64;
     MRYRDVMATA LIMSLALAGA AGAKQGAVPV HADSNLTETA DAFFKGQSTG GVVLVTRGDQ
     VLLRRAYGLS DVENAVPMRP DSALRLASIS KQFTAVAVLQ LVQAGKLGLD STLASLDPAL
     AGPMAGVTVQ QLLTHTSGIK NISGIAASRA ARREDADATR LIGYFKDLPL EFAPGSQFRY
     SNSNYILLTH LIERLDGRPY PQYMQQAVFQ PLGMSHTRYD NHLALIPRRA HGYRRVKGEL
     QNADFISMSQ PQGAGGLIST VDDLAIWHRA LRDGRLVPPA LFAQATGKTT LTNGRLSPYG
     FGWIIGQVGD LPDVEHGGFI NGFNSYVVRV KAPDVFVAVL TNAEFMDPTN LSVRLAAIAA
     GRPYPAEDTT RKTDTSWTGR YVFADGGARV VLEKDDALQL QQEGDDPVAL HPHRDGRHYL
     DGGLDSLEFG HDAQGRATIT LHDRLMGDSI GVRANQSANA PKNAAATDST GP
//
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