ID   A0A1W1XYT6_9NEIS        Unreviewed;       482 AA.
AC   A0A1W1XYT6;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase / D-alanyl-D-alanine-endopeptidase (Penicillin-binding protein 4) {ECO:0000313|EMBL:SMC29017.1};
GN   ORFNames=SAMN02745857_03537 {ECO:0000313|EMBL:SMC29017.1};
OS   Andreprevotia lacus DSM 23236.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chitinibacteraceae; Andreprevotia.
OX   NCBI_TaxID=1121001 {ECO:0000313|EMBL:SMC29017.1, ECO:0000313|Proteomes:UP000192761};
RN   [1] {ECO:0000313|EMBL:SMC29017.1, ECO:0000313|Proteomes:UP000192761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23236 {ECO:0000313|EMBL:SMC29017.1,
RC   ECO:0000313|Proteomes:UP000192761};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S13 family.
CC       {ECO:0000256|ARBA:ARBA00006096}.
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DR   EMBL; FWXD01000028; SMC29017.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W1XYT6; -.
DR   STRING; 1121001.SAMN02745857_03537; -.
DR   OrthoDB; 9802627at2; -.
DR   Proteomes; UP000192761; 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; 2.
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:SMC29017.1};
KW   Hydrolase {ECO:0000313|EMBL:SMC29017.1};
KW   Protease {ECO:0000313|EMBL:SMC29017.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192761};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..482
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012867985"
SQ   SEQUENCE   482 AA;  51953 MW;  DA04CCA16E0E1A20 CRC64;
     MLLRTTLAAL CCAAFSLAAS AADSLPASVQ AALKANKLPA DGLSVAIVAL NDGKPVLQYQ
     AERPVNPAST MKLVTTYSAL GLLGPAWQWQ TDLLSDAQPV NGVLNGNLYL RGSGDPKLTI
     ERVWQWLRDL KAAGVTDIKG KLVLDRSLFM LPPDSGFDDD GNGAERPFMV DPDAALTNFK
     SIRLLIDSTG DRVRLTAEPP LPEVRVSNEL AIGRSGNCEA WSQRVNQRLG QMNNLQITLQ
     LAGEVPAGCR VERYVAVMNA QTYTAALVRQ LWRELGGQGI AGWSEGATPA SALVLASTKS
     QDVANTIRDI NKYSNNMMAR QLFLTLGAQS QESGDTPTRA ATAIKSWLGQ QGLRFDELTL
     ENGSGLSRHE RISSAHLAQL LVSANRSRFA AEFISSLPIV AIDGTMRKRL KRDDIAAHIK
     TGTLKDVKAV AGYVRDADGV DWAVVAIANH PRAPQYAPVL DEILRWIANA PTSELAALRA
     TR
//