ID   U2ZIY7_VIBPR            Unreviewed;       474 AA.
AC   U2ZIY7;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase DacB {ECO:0000313|EMBL:GAD67726.1};
GN   Name=dacB {ECO:0000313|EMBL:GAD67726.1};
GN   ORFNames=VPR01S_09_01010 {ECO:0000313|EMBL:GAD67726.1};
OS   Vibrio proteolyticus NBRC 13287.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1219065 {ECO:0000313|EMBL:GAD67726.1, ECO:0000313|Proteomes:UP000016570};
RN   [1] {ECO:0000313|EMBL:GAD67726.1, ECO:0000313|Proteomes:UP000016570}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 13287 {ECO:0000313|EMBL:GAD67726.1,
RC   ECO:0000313|Proteomes:UP000016570};
RA   Isaki S., Hosoyama A., Numata M., Hashimoto M., Hosoyama Y., Tsuchikane K.,
RA   Noguchi M., Hirakata S., Ichikawa N., Ohji S., Yamazoe A., Fujita N.;
RT   "Whole genome shotgun sequence of Vibrio proteolyticus NBRC 13287.";
RL   Submitted (SEP-2013) 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:GAD67726.1}.
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DR   EMBL; BATJ01000009; GAD67726.1; -; Genomic_DNA.
DR   RefSeq; WP_021705697.1; NZ_BATJ01000009.1.
DR   AlphaFoldDB; U2ZIY7; -.
DR   STRING; 1219065.VPR01S_09_01010; -.
DR   MEROPS; S13.001; -.
DR   eggNOG; COG2027; Bacteria.
DR   Proteomes; UP000016570; 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:GAD67726.1};
KW   Hydrolase {ECO:0000313|EMBL:GAD67726.1};
KW   Protease {ECO:0000313|EMBL:GAD67726.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016570};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..474
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004638504"
SQ   SEQUENCE   474 AA;  52444 MW;  65580217A3057F65 CRC64;
     MTRTLNYALL LVSTLLAGQA IADKYAPVDK LPQGSRSSLL VEDLQGNNGL TLTNNSDQFF
     PPASTLKLVT ALAAKLELGD QFHYQTTLAK AGNDLVFQFS GDPTLTTKDL ANMLSAAKQQ
     KLTRITGDIW LDDSAFSGYE RAIGWPWDIL GVCYSAPASA ITLDENCIQA SIYTQDNGKT
     RVYVPEQYPV YVSTSVKTVT RAGQKAAQCD LELLTHPDNH YQLRGCLVSR KQPLPLKFAV
     QDTRLYATRM IYTELNRLGI KLDGKVKVGR PNAPLQKTLA VHYSAPLPQL LDEMLKKSDN
     LIADSLTKSL GAQFFIQPGS FKNGTAAIKQ IIFAHTGIDL KHAQLADGSG LSRNNRFTAH
     DMAAVLRYIY NNDHKLHIID MMPKAGESGT LHYRRSMRKA PIKGQMIAKS GSLYGSYNMA
     GYGLDKNGKP NAIFVQFVSD YHPVRRDDNQ PVVPPITQFE TLFYQDVINY SQAK
//