ID   A0A1X9LLK5_9MICO        Unreviewed;       471 AA.
AC   A0A1X9LLK5;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:ARJ06063.1};
GN   ORFNames=B5808_13160 {ECO:0000313|EMBL:ARJ06063.1}, GCM10010988_12430
GN   {ECO:0000313|EMBL:GGI37134.1};
OS   Cnuibacter physcomitrellae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Cnuibacter.
OX   NCBI_TaxID=1619308 {ECO:0000313|EMBL:ARJ06063.1, ECO:0000313|Proteomes:UP000192775};
RN   [1] {ECO:0000313|EMBL:ARJ06063.1, ECO:0000313|Proteomes:UP000192775}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XA {ECO:0000313|EMBL:ARJ06063.1}, and XA(T)
RC   {ECO:0000313|Proteomes:UP000192775};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GGI37134.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CGMCC 1.15041 {ECO:0000313|EMBL:GGI37134.1};
RX   PubMed=30832757;
RA   Wu L., Ma J.;
RT   "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT   project: providing services to taxonomists for standard genome sequencing
RT   and annotation.";
RL   Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN   [3] {ECO:0000313|EMBL:GGI37134.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CGMCC 1.15041 {ECO:0000313|EMBL:GGI37134.1};
RA   Sun Q., Zhou Y.;
RL   Submitted (DEC-2022) 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; CP020715; ARJ06063.1; -; Genomic_DNA.
DR   EMBL; BMHD01000001; GGI37134.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X9LLK5; -.
DR   STRING; 1619308.B5808_13160; -.
DR   KEGG; cphy:B5808_13160; -.
DR   Proteomes; UP000192775; Chromosome.
DR   Proteomes; UP000633908; Unassembled WGS sequence.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 2.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR000667; Peptidase_S13.
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:ARJ06063.1};
KW   Hydrolase {ECO:0000313|EMBL:ARJ06063.1};
KW   Protease {ECO:0000313|EMBL:ARJ06063.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192775}.
FT   REGION          217..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   471 AA;  47101 MW;  C0D477BF5551A5ED CRC64;
     MAGGVWGVVR RHPRAWLAGA ATVAFVLVGG SAFAVGTAVG GEESAPAPAA VAATATVTPE
     PTPTQRPQPQ AAPVGGPVRT CSIAEEASDG RLGTFLGQVR DASTGEVLFD RNGSTPARTA
     SVMKVLTSAA ALAVLGPDHR VPTTVVKGSA PGQVVLVGGG DITLASGSSN IYAGSASMLD
     LAAQVSQAWS ADPTTAGTPI TSIVLDASVF SGDRWQPSWN RKEQRDGYSS EVTGLQVDGD
     RADPSANVSA RSDDAVASAG QAFAAALGVS ASLSEGVAPA GAPQLGQVLS APVSTMIPDA
     LLRSDNTEAE MLARLVAVEL GVGNDFAALN VAIPQALATY GLDTSGLTIV DGSGLSDDNG
     VPPDFLTRLF TKIQAQEGNL SVIYHGLPVA GETGTLAGRF GGAASVAAGH VIAKTGWIDT
     GYTLSGIIQA ADGSVLTFAF YALDDVGDSA RAALDTLTAA AYSCGAGLSN R
//