ID   K0IFQ5_9BURK            Unreviewed;       491 AA.
AC   K0IFQ5;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:AFU48201.1};
GN   ORFNames=C380_22545 {ECO:0000313|EMBL:AFU48201.1};
OS   Acidovorax sp. KKS102.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=358220 {ECO:0000313|EMBL:AFU48201.1, ECO:0000313|Proteomes:UP000006306};
RN   [1] {ECO:0000313|EMBL:AFU48201.1, ECO:0000313|Proteomes:UP000006306}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KKS102 {ECO:0000313|EMBL:AFU48201.1,
RC   ECO:0000313|Proteomes:UP000006306};
RX   PubMed=23209225; DOI=10.1128/JB.01848-12;
RA   Ohtsubo Y., Maruyama F., Mitsui H., Nagata Y., Tsuda M.;
RT   "Complete Genome Sequence of Acidovorax sp. Strain KKS102, a
RT   Polychlorinated-Biphenyl Degrader.";
RL   J. Bacteriol. 194:6970-6971(2012).
CC   -!- SIMILARITY: Belongs to the peptidase S13 family.
CC       {ECO:0000256|ARBA:ARBA00006096}.
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DR   EMBL; CP003872; AFU48201.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0IFQ5; -.
DR   STRING; 358220.C380_22545; -.
DR   MEROPS; S13.003; -.
DR   KEGG; ack:C380_22545; -.
DR   PATRIC; fig|358220.3.peg.4603; -.
DR   eggNOG; COG2027; Bacteria.
DR   HOGENOM; CLU_017692_2_1_4; -.
DR   OrthoDB; 9802627at2; -.
DR   Proteomes; UP000006306; 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; 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:AFU48201.1};
KW   Hydrolase {ECO:0000313|EMBL:AFU48201.1};
KW   Protease {ECO:0000313|EMBL:AFU48201.1}.
SQ   SEQUENCE   491 AA;  52290 MW;  9FC90582FF456306 CRC64;
     MLSVSALWRR RVLRGVVGWG AAWLMAAGGV GSAGAQTAAP AAGTLPPEVE AALARAKLPR
     ESLSVMVVDA QAVGKASPRL AHRAQVPVNP ASVMKLVTTY AALEQLGPAY VWNTPVYVQG
     TVQDGSLRGN VYIQGQGDPK LVMERLWLLM RRLQGQGIQV IVGDIVLDRT AFDVPDQDPA
     RFDGEPLRPY NASPDALLLN YKSSVMTFVP DAAAGLARIQ YDPPLAGVQR QPTVALAAPG
     ADCGDWRTAL RAELSDPSKV SFQGVYPAAC GERVWPVAAA DPRGFAARAV EGMWRDLGGK
     LTGSVRDGKV PPGLKPAFVV TSPALSEVVR DVNKYSNNVM AQQVFLTLAL QKNGVATFDG
     AREVLRQWWQ ARMGDADLPQ VDNGAGLSRD ARLTAQALAR MLQVAWVSPV MPELVASLPI
     TGVDGTLRRS QSRAGTAHLK TGSLRDVMAV AGYVHAASGR RYVLVAVVNH PNAGAARPVL
     DSLIDWTARE Q
//