ID   A0A1H3CX78_9BURK        Unreviewed;       475 AA.
AC   A0A1H3CX78;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase / D-alanyl-D-alanine-endopeptidase (Penicillin-binding protein 4) {ECO:0000313|EMBL:SDX58049.1};
GN   ORFNames=SAMN04515617_1055 {ECO:0000313|EMBL:SDX58049.1};
OS   Collimonas sp. OK242.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Collimonas.
OX   NCBI_TaxID=1798195 {ECO:0000313|EMBL:SDX58049.1, ECO:0000313|Proteomes:UP000198586};
RN   [1] {ECO:0000313|EMBL:SDX58049.1, ECO:0000313|Proteomes:UP000198586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK242 {ECO:0000313|EMBL:SDX58049.1,
RC   ECO:0000313|Proteomes:UP000198586};
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; FNOR01000005; SDX58049.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3CX78; -.
DR   STRING; 1798195.SAMN04515617_1055; -.
DR   OrthoDB; 9802627at2; -.
DR   Proteomes; UP000198586; 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:SDX58049.1};
KW   Hydrolase {ECO:0000313|EMBL:SDX58049.1};
KW   Protease {ECO:0000313|EMBL:SDX58049.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..475
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011673541"
SQ   SEQUENCE   475 AA;  50943 MW;  51B1C5D0097DD52A CRC64;
     MNKIHAISLL ILSSALLSGV QAQESSAALP APFSKALQLA GIPAQSVGVY VQEVDGTGTV
     LASANAGVPF NPASTMKLVT TDAALELLGP TYRWKTQAYS NGSQAGNVLQ GDLIFKGNGD
     PKLVLENFWL FLRQIRAKGI RDIRGNIVLD RSTFDENAYD PAEFDGDPTK PYNVGPDALL
     LNYKTLTFQF VPNLETRQVN VLTDPPMSGY PVTPPRLGSG NCDDWQGKLQ ATVDADGASF
     NGALPASCGE KTWYLNPYKM SSTQYFGAVF RQMWADLGGT FSGVVKSGAM PAGSSLISEW
     SSVTLPEVIR DINKYSNNVM ARQVLLTIAS DILKVPATPE RGARAIQSWL TSKGIDASGL
     VIENGSGLSR NERISAKTMG RMMASAFQSP TMPEFVSSMP LVGYDGTMRK RLKNQTVAGQ
     AHVKTGTLND VRAIAGYVLA ASGKYYAVVC LINHPNAPRG QAAQDGLLQW VYENG
//