ID   A0A1I2X128_9BACT        Unreviewed;       464 AA.
AC   A0A1I2X128;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase / D-alanyl-D-alanine-endopeptidase (Penicillin-binding protein 4) {ECO:0000313|EMBL:SFH07250.1};
GN   ORFNames=SAMN05421739_105324 {ECO:0000313|EMBL:SFH07250.1};
OS   Pontibacter chinhatensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Pontibacter.
OX   NCBI_TaxID=1436961 {ECO:0000313|EMBL:SFH07250.1, ECO:0000313|Proteomes:UP000198724};
RN   [1] {ECO:0000313|EMBL:SFH07250.1, ECO:0000313|Proteomes:UP000198724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LP51 {ECO:0000313|EMBL:SFH07250.1,
RC   ECO:0000313|Proteomes:UP000198724};
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FOOT01000005; SFH07250.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2X128; -.
DR   STRING; 1436961.SAMN05421739_105324; -.
DR   OrthoDB; 9802627at2; -.
DR   Proteomes; UP000198724; Unassembled WGS sequence.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.710.10; 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:SFH07250.1};
KW   Hydrolase {ECO:0000313|EMBL:SFH07250.1};
KW   Protease {ECO:0000313|EMBL:SFH07250.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..464
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011555224"
SQ   SEQUENCE   464 AA;  51208 MW;  5DF55E1BCC90B65D CRC64;
     MKRLNQKITL TLALLLLHTF AWAQTVPEKV TAAYQAFEQD PQLQNAISSL YITDAKTGKV
     IFDKNSRIGL APASTMKLIT SISAYELLGT DFKYETKFAY RKGKGPAELL ILPSGDPTLG
     SWRWPETKEG EVLQGLTRAL QKTGVKSFGS VLVANEGWND ETVPDGWMWQ DIANYYGAGP
     AKLNWRENQY DVILQSGAKI GDPVAIVKTV PALNGYTLHS ELTAAAAGTG DNAYIYFPLS
     TSAATIRGTI PVNESSFKIS GAMPSASRQF VSTLSDTLRT VGIKLPKSVT EHHLALPYND
     YTVFHTITSP PLDSIIYWFN RRSINLYGEA LVKTIAAKHT PDSRTSNGLK EIRAFWKEWG
     LPETELSMVD GSGLSPLNRV TTHAQVQLLQ HARLQPWYNG IYASLPVFNG MKMKSGTIRG
     VKGFCGYHKS ADGKEYVFSF IVNNYNGSAS ALVKKMYKVL DELK
//