ID   A0A0M2Y2K7_9SPHI        Unreviewed;       466 AA.
AC   A0A0M2Y2K7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:KKO92661.1};
GN   ORFNames=AAW12_04180 {ECO:0000313|EMBL:KKO92661.1};
OS   Sphingobacterium sp. Ag1.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=1643451 {ECO:0000313|EMBL:KKO92661.1, ECO:0000313|Proteomes:UP000034524};
RN   [1] {ECO:0000313|EMBL:KKO92661.1, ECO:0000313|Proteomes:UP000034524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ag1 {ECO:0000313|EMBL:KKO92661.1,
RC   ECO:0000313|Proteomes:UP000034524};
RA   Pei D., Yu W., Kukutla P., Xu J.;
RT   "Draft Genome Sequences of Sphingobacterium sp. Ag1 from Mosquito Anopheles
RT   gambiae.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S13 family.
CC       {ECO:0000256|ARBA:ARBA00006096}.
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:KKO92661.1}.
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DR   EMBL; LBGU01000024; KKO92661.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M2Y2K7; -.
DR   PATRIC; fig|1643451.3.peg.3175; -.
DR   Proteomes; UP000034524; Unassembled WGS sequence.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.50.80.20; D-Ala-D-Ala carboxypeptidase C, peptidase S13; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR000667; Peptidase_S13.
DR   NCBIfam; TIGR00666; PBP4; 1.
DR   PANTHER; PTHR30023; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR30023:SF0; PENICILLIN-SENSITIVE CARBOXYPEPTIDASE A; 1.
DR   Pfam; PF02113; Peptidase_S13; 1.
DR   PRINTS; PR00922; DADACBPTASE3.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:KKO92661.1};
KW   Hydrolase {ECO:0000313|EMBL:KKO92661.1};
KW   Protease {ECO:0000313|EMBL:KKO92661.1}.
SQ   SEQUENCE   466 AA;  50792 MW;  C748F15F92515ACF CRC64;
     MAFSAYTLTT VATPVYAQDL RSKIQDAFTQ FQNQENLRNG LSSLTVFDAK TGQTVFAANE
     NVGLATASTM KVITSATALD FLGKNFQFKT TLYYTGEIDE NGVLNGNIIV TGTGDPTLGS
     ARYPETQATT ILNKWLTAVQ NAGIKSINGA IIADDRLYNG NQLPGGWIWT DMGNYYGAGI
     SSLNWCENAF GINFLPSTKV GAKAEIANYT TPVPYLEIIN ETTTGKTGSG DNVYAYAAPY
     STKIFVRGTY GQDLKKTIEL SSPDPAYDLA YQLNEVLSNN GITASELPAT GTKMDSVDIS
     KKQTLDIHLS PTLDKIVYWF NQKSINLYGE ALLKAIAYTT AGKTGTDDGA YYVQKYWNAK
     LGIKSSELNS MDGSGLSPQN RVTTSAMNKI MQYAQKQSWY PSFYESLPTY NNMKMKSGTI
     GGVLGYTGVH TNKTGQSFTY TLLVNNYAGS ASSMRQQMFK LLDVLK
//