ID   D8G4A8_9CYAN            Unreviewed;       476 AA.
AC   D8G4A8;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:CBN57448.1};
DE            EC=3.4.16.4 {ECO:0000313|EMBL:CBN57448.1};
GN   ORFNames=OSCI_3440001 {ECO:0000313|EMBL:CBN57448.1};
OS   Kamptonema sp. PCC 6506.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Microcoleaceae; Kamptonema.
OX   NCBI_TaxID=272129 {ECO:0000313|EMBL:CBN57448.1, ECO:0000313|Proteomes:UP000004532};
RN   [1] {ECO:0000313|EMBL:CBN57448.1, ECO:0000313|Proteomes:UP000004532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6506 {ECO:0000313|EMBL:CBN57448.1,
RC   ECO:0000313|Proteomes:UP000004532};
RX   PubMed=20675499; DOI=10.1128/JB.00704-10;
RA   Mejean A., Mazmouz R., Mann S., Calteau A., Medigue C., Ploux O.;
RT   "The genome sequence of the cyanobacterium Oscillatoria sp. PCC 6506
RT   reveals several gene clusters responsible for the biosynthesis of toxins
RT   and secondary metabolites.";
RL   J. Bacteriol. 192:5264-5265(2010).
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:CBN57448.1}.
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DR   EMBL; CACA01000308; CBN57448.1; -; Genomic_DNA.
DR   RefSeq; WP_007356648.1; NZ_CACA01000308.1.
DR   AlphaFoldDB; D8G4A8; -.
DR   MEROPS; S13.002; -.
DR   OrthoDB; 9802627at2; -.
DR   Proteomes; UP000004532; Unassembled WGS sequence.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
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:CBN57448.1};
KW   Hydrolase {ECO:0000313|EMBL:CBN57448.1};
KW   Protease {ECO:0000313|EMBL:CBN57448.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004532};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..476
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003114525"
SQ   SEQUENCE   476 AA;  52071 MW;  2DAB042096649362 CRC64;
     MKGIGISLLL VIIGWPLTAV AQRQAAENIC PAQLGVAVDA IANRAQFRRS RWGMVIQTLS
     TATTLYSRDA QQYFIPASNV KLLTTAAALQ KLGPQFRIRT SVYGDQNRRL YIVGRGDPSI
     TETQLKDLAK QLKQRGVNQV SELIADDSYF PGDSVNRNWE WEDVQAGYGA PINSLIFNEN
     AIKLVLSPQS IGQPLRVTFA DVTQANQWRI ENNSVTVGKD ESEFVEVGRD FWQPIIRVRG
     NLRFGSESEF AYVSVVNPAN NFLQRFRQVL NAEGITVKQA LVASNFSPQT QELAAVESPL
     LADLVRETNQ ESVNIYAEVL VRLLGKIAPL PRKDRVGFGL PELAAALTQL GVNPDGYVLA
     DGSGLSRQNL VSPEALVQTL RLMANSPVKS IYRDSLPVAG TSGTLKNRFN NTSAQGIVRA
     KTGTLTGVSA LSGYVEVANF EPLAFSIIVN QSDLSAGDLR EAIDEIVLVL TRLKRC
//