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Database: UniProt
Entry: A0A291Q9J2_9ACTN
LinkDB: A0A291Q9J2_9ACTN
Original site: A0A291Q9J2_9ACTN 
ID   A0A291Q9J2_9ACTN        Unreviewed;       530 AA.
AC   A0A291Q9J2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:ATL28143.1};
DE            EC=3.4.16.4 {ECO:0000313|EMBL:ATL28143.1};
GN   ORFNames=KY5_3125c {ECO:0000313|EMBL:ATL28143.1};
OS   Streptomyces formicae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1616117 {ECO:0000313|EMBL:ATL28143.1, ECO:0000313|Proteomes:UP000221011};
RN   [1] {ECO:0000313|EMBL:ATL28143.1, ECO:0000313|Proteomes:UP000221011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KY5 {ECO:0000313|EMBL:ATL28143.1,
RC   ECO:0000313|Proteomes:UP000221011};
RA   Holmes N.A., Devine R., Qin Z., Seipke R.F., Wilkinson B., Hutchings M.I.;
RT   "Complete Genome Sequence of Streptomyces formicae KY5, the formicamycin
RT   producer.";
RL   Submitted (AUG-2017) 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; CP022685; ATL28143.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A291Q9J2; -.
DR   KEGG; sfk:KY5_3125c; -.
DR   Proteomes; UP000221011; Chromosome.
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:ATL28143.1};
KW   Hydrolase {ECO:0000313|EMBL:ATL28143.1};
KW   Protease {ECO:0000313|EMBL:ATL28143.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000221011};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           37..530
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012945637"
SQ   SEQUENCE   530 AA;  55979 MW;  201FE1A752902E64 CRC64;
     MSRPVRRVPA RMRHWIWPAV LGVAAATLSW SAPAGAESDR SGLPEAIDTI LGDPRMDGGA
     ASVVIADAAS GDVLYQRQPS GRLVPASSTK MLTSAAAMAL LGPDHRFTTD VLADGERHGR
     VLRGDLYLRG TGDPTTLAED YDQLAAKVAD SGIRKVSGRL VADDTRFDDH RIGDTWGGDD
     ESSYYAAQIS ALSVAPDTDY DTGTVIVEVA PGRRAGDRPR VSVTPKTDYV DIDLRASTVA
     AGGRDTIAVE RRHGENTLTV SGTVPVGAAP AKEWVTVWEP TGYAAAVFRD ALTAHGVRVT
     GPTRTGVAAP RSARQLATHD SMALKDLLIP FMKLSNNMHA ESLTKAMGYE ATGRPGSWGD
     GIEAIGGYLK GIGVDPGTLR QVDGSGLSRK NLAPAGQYVK LLRAVRGEPW FADWYASLSV
     ACVPDKFVGG SLRSRMCGTP AAGNARAKVG SLTGASALSG YVTDKDGREL VFSIILNNYL
     AASVKPLEDA IVVTLASSTE DEAVLVKPRS TRGAERAGEL ECAWRKPARC
//
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