ID A0A0G3UYM5_9ACTN Unreviewed; 505 AA.
AC A0A0G3UYM5;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:AKL70160.1};
GN ORFNames=M444_19465 {ECO:0000313|EMBL:AKL70160.1};
OS Streptomyces sp. Mg1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=465541 {ECO:0000313|EMBL:AKL70160.1, ECO:0000313|Proteomes:UP000035653};
RN [1] {ECO:0000313|EMBL:AKL70160.1, ECO:0000313|Proteomes:UP000035653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mg1 {ECO:0000313|EMBL:AKL70160.1,
RC ECO:0000313|Proteomes:UP000035653};
RX PubMed=23908282;
RA Hoefler B.C., Konganti K., Straight P.D.;
RT "De Novo Assembly of the Streptomyces sp. Strain Mg1 Genome Using PacBio
RT Single-Molecule Sequencing.";
RL Genome Announc. 1:e00535-13(2013).
CC -!- SIMILARITY: Belongs to the peptidase S13 family.
CC {ECO:0000256|ARBA:ARBA00006096}.
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DR EMBL; CP011664; AKL70160.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3UYM5; -.
DR KEGG; strm:M444_19465; -.
DR PATRIC; fig|465541.12.peg.4153; -.
DR Proteomes; UP000035653; Chromosome.
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; 2.
DR PRINTS; PR00922; DADACBPTASE3.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:AKL70160.1};
KW Hydrolase {ECO:0000313|EMBL:AKL70160.1};
KW Protease {ECO:0000313|EMBL:AKL70160.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035653}.
FT REGION 39..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 505 AA; 50211 MW; 20E5BB19E6EAFB44 CRC64;
MRDRERGWSE VPLVKTWQLI AASAVAGLVL SAATVSVTGP WDSGQRKAER DRAASWSRMG
GVDHGSGRLP EAAPSAPGVL SGLAAALQAE KQAGNPLGEQ AGRQPGTGTG EGTGSGSDAL
AGALRPLFAD PALGSLRSAS VIDTATGRVL YEAKPREPMT PASTVKIATA TAVLAALGPE
HRFRTTVTPG AAPGQIILVG GGDPSLTARK KPPAGSGGSL VALAADTAQA LKAAGTDSVS
LGYDDSLYSG PARHPIGLNP NVAPLSALTA DEGRLNDSLS GPADRSEDPS GDTARAFADL
LADRGIKVTG APAKARAAAD AEPLATTLST PLGGLVERML TNSDNDIAEA LARQSALASG
QPGSFEGAGK AVAATLASLG IDTTGARFAD GSGLDRSDKV SAGLLTALLA KAADPQRPEL
RPVLTGLPVA GFNGTLRSRN SGGSPAAGLV RAKTGTLSGV NALAGTVVDP SGRLLAFAFL
AANTPGPEGA EKALDKLAAA VAGTR
//