ID   R5UWM6_9BACT            Unreviewed;       460 AA.
AC   R5UWM6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:CCZ82470.1};
GN   ORFNames=BN709_01742 {ECO:0000313|EMBL:CCZ82470.1};
OS   Odoribacter laneus CAG:561.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Odoribacteraceae;
OC   Odoribacter.
OX   NCBI_TaxID=1263089 {ECO:0000313|EMBL:CCZ82470.1, ECO:0000313|Proteomes:UP000017974};
RN   [1] {ECO:0000313|EMBL:CCZ82470.1, ECO:0000313|Proteomes:UP000017974}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:561 {ECO:0000313|Proteomes:UP000017974};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CCZ82470.1}.
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DR   EMBL; CBAQ010000108; CCZ82470.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5UWM6; -.
DR   MEROPS; S13.002; -.
DR   Proteomes; UP000017974; 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   Carboxypeptidase {ECO:0000313|EMBL:CCZ82470.1};
KW   Hydrolase {ECO:0000313|EMBL:CCZ82470.1};
KW   Protease {ECO:0000313|EMBL:CCZ82470.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017974}.
SQ   SEQUENCE   460 AA;  50906 MW;  20C9E3DAFB7CDE43 CRC64;
     MKQSLKFFGG LWMVLCLGAT ALYAQPGLAL ERLLANAGLR NAVMGIAIRD CADGKEVFNY
     QGQLALHPAS VAKLLPSAWA LEKRGADFCF KTRVFYSGGI REHAIEGDVV IVPSGDPTPD
     SRYFPDSCFI RKFVSVLREK GIYTIKGRII VQGESEEEIP GSWPWEDISN YYGALCHRFN
     YRDNTYCLNF TTGAAGTTAR LLSVEPALSE IRFRNQVKAA ASGGDNAWIY GGPYSNVLYV
     KGTLPTHQAS FQVKGAMHQP EKYFIAELTT YLKKEGIKIE QRIPRNTTLE ELWVYTSPLL
     EEIVFHTNKS SVNLFAEALG QLMAPFQYER ALKQWLSGQG IDTSGILLKD ACGLSPQNAI
     PAETIAHLLY TQRNNTAWVR SLPVAGTDRG LNVYLRHHPV LKNKLSAKTG SFSGVRCLAG
     YLTTSSGKRL AFAFFINNYT CPAAVVYEAV GAFLSDWVSY
//