ID   A0A0Q8DMR4_9ACTN        Unreviewed;       492 AA.
AC   A0A0Q8DMR4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASD81_19730 {ECO:0000313|EMBL:KRA29931.1};
OS   Nocardioides sp. Root614.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1736571 {ECO:0000313|EMBL:KRA29931.1, ECO:0000313|Proteomes:UP000051699};
RN   [1] {ECO:0000313|EMBL:KRA29931.1, ECO:0000313|Proteomes:UP000051699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root614 {ECO:0000313|EMBL:KRA29931.1,
RC   ECO:0000313|Proteomes:UP000051699};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRA29931.1, ECO:0000313|Proteomes:UP000051699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root614 {ECO:0000313|EMBL:KRA29931.1,
RC   ECO:0000313|Proteomes:UP000051699};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KRA29931.1}.
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; LMGV01000008; KRA29931.1; -; Genomic_DNA.
DR   RefSeq; WP_056715613.1; NZ_LMGV01000008.1.
DR   AlphaFoldDB; A0A0Q8DMR4; -.
DR   Proteomes; UP000051699; 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; 2.
DR   PRINTS; PR00922; DADACBPTASE3.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000051699}.
SQ   SEQUENCE   492 AA;  49975 MW;  A8214D21E8F3440F CRC64;
     MASRDEERVS GRRKKAFGGL VAVALVAAGG VAWQTGWAED QWHDFRNGQS GVPADPAAVA
     PPPEVDVPDV VLPSAVAEPA NGLGQLDPGA VEQALAGLND PDLGRHVLAI VGALDGTGVA
     YERSEGAAVA IPASTTKVVT SAVALFLLGP DKVFTTTTVL DQTGTTPRLT LVGGGDPFLS
     RSPETASGAG SATFVPVRAN IRTLARRTAR ALKADGIRSV ELAYDDSLFS GPAVNPHWEP
     SYVPDDIAPI GALWVDQGRE ADGSGRVANP PATAAEEFRK ALVRYGVKAV GRTTHAAAAA
     AATPVGSVSS PTVAQIVQRL IEVSDNAAAE VLLRHIGIAD QGAGSFEAGQ AGVKRVLAAN
     GVPLGASVLY DGSGLSRANR LAPAVLLGVL RLAASDAHPQ LRPLLAALPV AGFTGSLANR
     MDKGPAAARG RVRAKTGTLS NVSSLAGIAL DRDGNLMGFV LMADRIKDPK ETLAQTALDN
     AAAGLGACSC GG
//