ID   A0A0D8ZT33_9CYAN        Unreviewed;       497 AA.
AC   A0A0D8ZT33;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:KJH71923.1};
GN   ORFNames=UH38_09325 {ECO:0000313|EMBL:KJH71923.1};
OS   Aliterella atlantica CENA595.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Chroococcidiopsidales;
OC   Aliterellaceae; Aliterella.
OX   NCBI_TaxID=1618023 {ECO:0000313|EMBL:KJH71923.1, ECO:0000313|Proteomes:UP000032452};
RN   [1] {ECO:0000313|EMBL:KJH71923.1, ECO:0000313|Proteomes:UP000032452}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CENA595 {ECO:0000313|EMBL:KJH71923.1,
RC   ECO:0000313|Proteomes:UP000032452};
RA   Rigonato J., Alvarenga D.O., Branco L.H., Varani A.M., Brandini F.P.,
RA   Fiore M.F.;
RT   "Draft genome of a novel marine cyanobacterium (Chroococcales) isolated
RT   from South Atlantic Ocean.";
RL   Submitted (FEB-2015) 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:KJH71923.1}.
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DR   EMBL; JYON01000008; KJH71923.1; -; Genomic_DNA.
DR   RefSeq; WP_045054491.1; NZ_JYON01000008.1.
DR   AlphaFoldDB; A0A0D8ZT33; -.
DR   STRING; 1618023.UH38_09325; -.
DR   PATRIC; fig|1618023.3.peg.3609; -.
DR   OrthoDB; 9802627at2; -.
DR   Proteomes; UP000032452; 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:KJH71923.1};
KW   Hydrolase {ECO:0000313|EMBL:KJH71923.1};
KW   Protease {ECO:0000313|EMBL:KJH71923.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032452}.
SQ   SEQUENCE   497 AA;  53418 MW;  2BEEC7EF909466CD CRC64;
     MTKQTSLVLI LLNAQFSISQ PVAAKRNIQG IYAQSALPDL LKSPNSVCPA QLGTAIDRII
     DRPQFSRSRW GIVVQKLNNA QNLYSRDADK YFIPASNLKL LTTAAALQKL GANFRFRTSI
     YGTDDGLLRL VGRGDPSLTD VQLTALARQL KLTGVRQLIY LGVEGDRADD IISPDWEWGD
     IQADYGAPIG SLILNQNAVT LQLLPQQVNQ PLRLVWQDPI AARMWQVDNQ SVTAKPKSPA
     EVVVNRDLSG ILQISGQLSA DSPPESVALA VVNPAENFVQ HLRRVLLVAG IADNSDRVRL
     NIIEVQKQLA KAPELAAINS SPLSQLLIET NQNSNNLYAE ALLRALGSRV NSSNSNSQKG
     IIAVKQALTT LGVDATGYVL ADGSGLSRHN LATPKAIAQT LNAMAKSPQA AIYRASLPIA
     GVSGTLKNRL QGTPAQGIVS AKTGTISGAI GLSGYIEAPN YEPLVFSIIV NQSDRPTTVL
     RQAVDEIVVN LASLRRC
//