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Database: UniProt
Entry: A0A167I949_9BURK
LinkDB: A0A167I949_9BURK
Original site: A0A167I949_9BURK 
ID   A0A167I949_9BURK        Unreviewed;       484 AA.
AC   A0A167I949;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:AOW15298.1};
DE   SubName: Full=Peptidase M15 {ECO:0000313|EMBL:OAD42359.1};
GN   ORFNames=LPB072_02140 {ECO:0000313|EMBL:AOW15298.1}, LPB72_08810
GN   {ECO:0000313|EMBL:OAD42359.1};
OS   Hydrogenophaga crassostreae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Hydrogenophaga.
OX   NCBI_TaxID=1763535 {ECO:0000313|EMBL:AOW15298.1, ECO:0000313|Proteomes:UP000185680};
RN   [1] {ECO:0000313|EMBL:OAD42359.1, ECO:0000313|Proteomes:UP000185657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LPB0072 {ECO:0000313|EMBL:OAD42359.1,
RC   ECO:0000313|Proteomes:UP000185657};
RA   Shin S.-K., Yi H.;
RT   "Draft genome sequence of Hydrogenophaga sp. LPB0072.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AOW15298.1, ECO:0000313|Proteomes:UP000185680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LPB0072 {ECO:0000313|EMBL:AOW15298.1,
RC   ECO:0000313|Proteomes:UP000185680};
RA   Kim E., Yi H.;
RT   "Hydorgenophaga sp. LPB0072 isolated from gastropod.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S13 family.
CC       {ECO:0000256|ARBA:ARBA00006096}.
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DR   EMBL; CP017476; AOW15298.1; -; Genomic_DNA.
DR   EMBL; LVWD01000009; OAD42359.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A167I949; -.
DR   STRING; 1763535.LPB072_02140; -.
DR   KEGG; hyl:LPB072_02140; -.
DR   Proteomes; UP000185657; Unassembled WGS sequence.
DR   Proteomes; UP000185680; Chromosome.
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:AOW15298.1};
KW   Hydrolase {ECO:0000313|EMBL:AOW15298.1};
KW   Protease {ECO:0000313|EMBL:AOW15298.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185680}.
SQ   SEQUENCE   484 AA;  52198 MW;  2628FF1AAF12B3B0 CRC64;
     MTLSPGLALP APRADTPLPA TVLAALTRAG VPASALSALV IPVNGAGSDR LRYQADRPVN
     PASVMKLVTT YAAMDMLGAD FTWRTDFYTD GQIDNGTLRG NLYVRGGGDP KLVLERIQDT
     FFALHSKGVQ VILGDMVLDH SSFDLPSHDP GEFDGESLRP YNASPDALLV NFKSVVLNFQ
     PDPKAGVAYV TSEPPMARLA IDATVPLSRS GCGNWRDTLQ ARFDDANTIR FEGRYPQRCG
     EKVWPVAYQE PDSYAERAFE GLWRASGGAI TGRVRVGLVP KEARLLHEAY SLPLTDIISD
     VNHWSNNVMA QQVFLTLGRL APPTRQEARS APIGTFTPLV TGRFERSREV VARWWRTSFG
     IRSTPPVLEN GSGLSRNERI TPQGLGDLLR HAARHPQSNK FIESLSVAGV NGTASRLARG
     SNSAARGNAW IKTGTLKDVT GIAGYVDATG GSRFAVVGFV NHANASAARP ALDALLEWAA
     SQPD
//
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