ID   A0A1X1MNC8_9VIBR        Unreviewed;       466 AA.
AC   A0A1X1MNC8;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ST37_16110 {ECO:0000313|EMBL:ORT48910.1};
OS   Vibrio sp. qd031.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1603038 {ECO:0000313|EMBL:ORT48910.1, ECO:0000313|Proteomes:UP000193432};
RN   [1] {ECO:0000313|EMBL:ORT48910.1, ECO:0000313|Proteomes:UP000193432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=qd031 {ECO:0000313|Proteomes:UP000193432};
RA   Xiang T., Song Y., Huang L., Wang B., Wu P.;
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ORT48910.1, ECO:0000313|Proteomes:UP000193432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=qd031 {ECO:0000313|Proteomes:UP000193432};
RA   Chen G.;
RT   "Denovo assembling a bacteria genome.";
RL   Submitted (MAY-2017) 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:ORT48910.1}.
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; JXQD01000029; ORT48910.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X1MNC8; -.
DR   STRING; 1603038.ST37_16110; -.
DR   OrthoDB; 9802627at2; -.
DR   Proteomes; UP000193432; 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; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000193432};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..466
FT                   /note="D-alanyl-D-alanine carboxypeptidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013117862"
SQ   SEQUENCE   466 AA;  51477 MW;  815EE4FA71D2F78D CRC64;
     MFKIFLTFFV FLFSATAWTA PFDGIEYLPA GSRAAIYVAS EQGADIIYNS EQLLPPASTL
     KILTALAAKI ELGDDFQFVT QLQKSNRDLF LSFSGDPKLA RTDIKKLLQE YKTQHGNIIP
     GNLYIDDRQF TGYEKAPGWP WDNLGVCYSA PSSVVTLDDN CIQGSISSLA TGQTRVYVPP
     HQPIEVSTDT ITLTKDQQKI QHCDLELTTF GNTYRLAGCM AERSKPLPLK FAIQDTRSYV
     SATLRGLLSE LNISLQGVII TRAKRDTPNE LTLVAEHRSP PLSDLLKIML QESDNLIADN
     VLKALGRSYY QAPGSFSNGA AAMKAILEYH TKTNLDYAQF FDGSGLSRNN KITASQLASV
     LQYIQLNDHT LNFIELLPTA GVDGTLKYRS SMRGDDVKGQ LAAKSGSLFG SINMAGFSLD
     AQGEPNKWFV QLIADYHPPQ SETPATPVEA PYTSFEKAFY RQLLTD
//