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Database: UniProt
Entry: A0A1I1PMA3_9BURK
LinkDB: A0A1I1PMA3_9BURK
Original site: A0A1I1PMA3_9BURK 
ID   A0A1I1PMA3_9BURK        Unreviewed;       527 AA.
AC   A0A1I1PMA3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase / D-alanyl-D-alanine-endopeptidase (Penicillin-binding protein 4) {ECO:0000313|EMBL:SFD10852.1};
GN   ORFNames=SAMN05216321_111172 {ECO:0000313|EMBL:SFD10852.1};
OS   Cupriavidus sp. OV038.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=1855313 {ECO:0000313|EMBL:SFD10852.1, ECO:0000313|Proteomes:UP000199583};
RN   [1] {ECO:0000313|EMBL:SFD10852.1, ECO:0000313|Proteomes:UP000199583}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV038 {ECO:0000313|EMBL:SFD10852.1,
RC   ECO:0000313|Proteomes:UP000199583};
RA   de Groot N.N.;
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; FOKX01000011; SFD10852.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1PMA3; -.
DR   Proteomes; UP000199583; 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; 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:SFD10852.1};
KW   Hydrolase {ECO:0000313|EMBL:SFD10852.1};
KW   Protease {ECO:0000313|EMBL:SFD10852.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..527
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011560526"
SQ   SEQUENCE   527 AA;  55709 MW;  AF4108CC17D38BA1 CRC64;
     MLAMPNRPAL LRLPLTAAIA AAVLLTTGIA GAQAKPAKPA KAAQAVKATA SKSASVRRAS
     ADTVDLAAAR TGLPASVTAA LRRANVPLSA ASFYVVKVGA PQARVSWNAE TPMNPASTMK
     VVTTFAGLQL LGPDYRWLTS LYADSEPTAD GTVRGNVYLR GRGDPKLVPE EMAKLVATAR
     NAGATTIDGD VVLDRSFFAD AAEGTYTIDG ESQRAYNVNP DALLYAFKTL SFTITPDAAG
     RTVDVAVTPA LAQLRVENRL TLTNGRCGDW RSRATPNIAP QPDGTVVATF EGTYSGDCGE
     RVVNLATLSH SDFIWGGFVA EWQAAGGRFA HMPGLRSGAV PRGAFLLSRH YGQPLGDVVR
     DINKFSNNVM ARQLFLTIGA EMDRSGPAST ARSAQVIRRW LTRQGLDMPG LVLDNGSGLS
     REERISAYDM ARLLQQALAS DVGYTLVDSL PILGVDGTLR NRLTRAHAAG NAYLKTGTLA
     DVRALAGYVD ATNGGRYVVV AYINHPNASG AQAAHDALME WVFRGAP
//
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