ID A0A0A0BL31_9CELL Unreviewed; 469 AA.
AC A0A0A0BL31;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:KGM08676.1};
GN ORFNames=N868_06880 {ECO:0000313|EMBL:KGM08676.1};
OS Cellulomonas carbonis T26.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=947969 {ECO:0000313|EMBL:KGM08676.1, ECO:0000313|Proteomes:UP000029839};
RN [1] {ECO:0000313|EMBL:KGM08676.1, ECO:0000313|Proteomes:UP000029839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T26 {ECO:0000313|EMBL:KGM08676.1,
RC ECO:0000313|Proteomes:UP000029839};
RA Chen F., Li Y., Wang G.;
RT "Genome sequencing of Cellulomonas carbonis T26.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGM08676.1, ECO:0000313|Proteomes:UP000029839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T26 {ECO:0000313|EMBL:KGM08676.1,
RC ECO:0000313|Proteomes:UP000029839};
RX PubMed=26587181;
RA Zhuang W., Zhang S., Xia X., Wang G.;
RT "Draft genome sequence of Cellulomonas carbonis T26(T) and comparative
RT analysis of six Cellulomonas genomes.";
RL Stand. Genomic Sci. 10:104-104(2015).
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:KGM08676.1}.
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DR EMBL; AXCY01000174; KGM08676.1; -; Genomic_DNA.
DR RefSeq; WP_043610266.1; NZ_AXCY01000174.1.
DR AlphaFoldDB; A0A0A0BL31; -.
DR OrthoDB; 56883at2; -.
DR Proteomes; UP000029839; 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 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; 2.
DR PRINTS; PR00922; DADACBPTASE3.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:KGM08676.1};
KW Hydrolase {ECO:0000313|EMBL:KGM08676.1};
KW Protease {ECO:0000313|EMBL:KGM08676.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029839}.
FT REGION 47..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 469 AA; 47260 MW; BA4BD860AF84C05D CRC64;
MSTTRVTAAV AGVVVLLGAG WVTADAYDVV PGVVTLDAPY PPPVPFPTAP GAVEPPGLLA
GPPEPTDPVP LPEADELRAL ADAVVAHRWI GESVGIVVAD GVTGEVLVDV GGATPREPAS
TAKLLTAVAA TSALGPDATV ETRVVQQGPG RIVLVGGGDV MLAAGAGDPD AINGRAGLAD
LADDTARALA LAGTTEVTLA LDDTLFSGPD VAPGWTPGDL ALGYMARVSP IAVNIAKTRE
EPYPPRHADP SMHAATTFAA LLRDRGVTVV GEPARATAPA SAVPLASVRS ATVREVVRYL
LHTSDNTVTE VVGRLVALDA GLPGSFQGAT RAVLAEVRGL GVDVEGAVLA DCSGLAEGSA
LPTSLLVDLM RVADADAQLR GVLVDLPVAG WQGTLGDRYG DLPARGLVRA KTGSLVGVTS
LAGTVVTQQG RHLLFAVVAD RTPPGGQLGP RRVVDAFVQQ LAGCACGLP
//
