ID   A0A1D9BHC5_9NEIS        Unreviewed;       479 AA.
AC   A0A1D9BHC5;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:AOY01881.1};
GN   ORFNames=BJP62_16365 {ECO:0000313|EMBL:AOY01881.1};
OS   Jeongeupia sp. USM3.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chitinibacteraceae; Jeongeupia.
OX   NCBI_TaxID=1906741 {ECO:0000313|EMBL:AOY01881.1, ECO:0000313|Proteomes:UP000176825};
RN   [1] {ECO:0000313|EMBL:AOY01881.1, ECO:0000313|Proteomes:UP000176825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USM3 {ECO:0000313|EMBL:AOY01881.1,
RC   ECO:0000313|Proteomes:UP000176825};
RA   Kho H.P.;
RT   "Jeongeupia sp. strain USM3 Genome sequencing and assembly.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AOY01881.1, ECO:0000313|Proteomes:UP000176825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USM3 {ECO:0000313|EMBL:AOY01881.1,
RC   ECO:0000313|Proteomes:UP000176825};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; CP017668; AOY01881.1; -; Genomic_DNA.
DR   RefSeq; WP_070531404.1; NZ_CP017668.1.
DR   AlphaFoldDB; A0A1D9BHC5; -.
DR   STRING; 1906741.BJP62_16365; -.
DR   KEGG; jeu:BJP62_16365; -.
DR   OrthoDB; 9802627at2; -.
DR   Proteomes; UP000176825; Chromosome.
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:AOY01881.1};
KW   Hydrolase {ECO:0000313|EMBL:AOY01881.1};
KW   Protease {ECO:0000313|EMBL:AOY01881.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..479
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009440355"
SQ   SEQUENCE   479 AA;  50929 MW;  07E33A0E04159B38 CRC64;
     MKPTIKQALL SLWLCAGAAN AALPVDVESA LAKAGVPASA LAAAILPVDG GPAVLLENAT
     RPMNPASTMK LVTTWSALNL LGPAYSWKTQ LLSDTPVANG VLNGPLYLRG SGDPKLTFER
     MWLLVRELRA AGVSEIRGDL VLDRSAFRLP VSTSAFDDDS DEAGQPYLVT PDALVSNFGS
     VRLMLRSDGS TVRATLEPAL DALRLDSSVK LAAGASCAGW KDGVQLRLDD AGQSARVSVA
     GRFPADCAGD RYFAVLDARS YTASLFRSLW QEQGGRFSGQ VRDGVTPPQA RLLATSISPP
     LTEAVRDINK FSNNLMARQL FLTLGATSPD PAGDTAAAAD ARVRGWLQQQ GLNMAELHLE
     NGAGLSRVER ISAEHLGRML VSAYRSPLAP EFISSLPIVG IDGTMKKRLK DEAGAAHIKT
     GTLKDVRAVA GYVRDQQGRD WVVVALLNHP KAPGAMPVLD ALLRWVATRS STEIAALRH
//