ID   A0A0L8LT42_9ACTN        Unreviewed;       535 AA.
AC   A0A0L8LT42;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=D-Ala-D-Ala carboxypeptidase {ECO:0000313|EMBL:KOG41367.1};
GN   ORFNames=ADK74_20390 {ECO:0000313|EMBL:KOG41367.1};
OS   Streptomyces decoyicus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=249567 {ECO:0000313|EMBL:KOG41367.1, ECO:0000313|Proteomes:UP000037606};
RN   [1] {ECO:0000313|Proteomes:UP000037606}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 2666 {ECO:0000313|Proteomes:UP000037606};
RG   Consortium for Microbial Forensics and Genomics (microFORGE);
RA   Knight B.M., Roberts D.P., Lin D., Hari K., Fletcher J., Melcher U.,
RA   Blagden T., Winegar R.A.;
RL   Submitted (JUL-2015) 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:KOG41367.1}.
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DR   EMBL; LGUU01000238; KOG41367.1; -; Genomic_DNA.
DR   RefSeq; WP_030079110.1; NZ_LGUU01000238.1.
DR   AlphaFoldDB; A0A0L8LT42; -.
DR   PATRIC; fig|249567.6.peg.4458; -.
DR   Proteomes; UP000037606; 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   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:KOG41367.1};
KW   Hydrolase {ECO:0000313|EMBL:KOG41367.1};
KW   Protease {ECO:0000313|EMBL:KOG41367.1}.
SQ   SEQUENCE   535 AA;  56215 MW;  3A603C66C0543CC8 CRC64;
     MSPSVPHRTA RRRLAGTVGV LLAVGVVITG LVQAAPSSAP PTLDPRITSI LRKPEYRHAQ
     WGLLQQNPET RKVTQSRSAD QFFIPGSTAK LFSVSATWHT LGGGHRFVTP VHAVGQRRGA
     TLRGDLDLVA QGDLTLGGRT RKDGTVDFTA IDHTYANDVP GATLTPQDPL AGLHHLAQHV
     RKSGIRRVDG DVVVDARLFR PDPALAPAPT PLIINDNLID LLTSPGARVG APAGLQWRPK
     VAPYHVTSAV RTVAAGKPAD ITVSSSADGT RIRLTGTIAA GSAPVLRVSA VKDPNAFGRT
     AMIEALKRAG VEVRAKAIGP NPSGQLPKSY QGAPAVARYT SPSYAQYAKL ILKVSHNLGA
     NLGICLMSTT TGSTNCEDGF PVLARFLEHA QVDRKAVQLA DGRGGNPADR TTPRALAQIL
     TYWQHTPDAL RFRTSLPILG VDGTLADSCH SCPSRGKVFA KTGTAAGGDT LNDRLAVGAE
     TAAGYLETRP GRFDVFFAGV NGASTPNADI NGVLAIGNDV ADVAAHLQQQ ASARH
//