ID A0A1Q4WBC6_9ACTN Unreviewed; 543 AA.
AC A0A1Q4WBC6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:OKI07284.1};
GN ORFNames=A6A06_35790 {ECO:0000313|EMBL:OKI07284.1};
OS Streptomyces sp. CB02923.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1718985 {ECO:0000313|EMBL:OKI07284.1, ECO:0000313|Proteomes:UP000185893};
RN [1] {ECO:0000313|EMBL:OKI07284.1, ECO:0000313|Proteomes:UP000185893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02923 {ECO:0000313|EMBL:OKI07284.1,
RC ECO:0000313|Proteomes:UP000185893};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKI07284.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LWKZ01000004; OKI07284.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q4WBC6; -.
DR STRING; 1718985.A6A06_35790; -.
DR Proteomes; UP000185893; 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:OKI07284.1};
KW Hydrolase {ECO:0000313|EMBL:OKI07284.1};
KW Protease {ECO:0000313|EMBL:OKI07284.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000185893}.
FT REGION 95..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 543 AA; 55416 MW; A334CC32F631E262 CRC64;
MPETRSLQVR WQAAQRLAQR SVRTAAGSAR SAGSAAVSMT RSAAGSARSA YRSAADSTRN
AWWSASKQQR QTVRLTASST VLGLLVSAGA VAAAGPWDSG QRTAERARAV APGDTRGEHH
VPGGTAPAPS APPVLAAIGV PPRAGSNGPP SAKGVAGVLA PLMKDDAFGS LRTASVVDAA
TGRELFGAEP GRNATPASTV KLAIATAALT ALGPEHRIDT TVVEGARGGL VLVGGGDPTL
TARAPEHGVQ DQPASLRTLA DDTARALKER GTGKVRLGYD LSAYTGPVLH PISPNENITP
VTSLMADEGR LDETRAGPAP RDTDPAATAA RTFAQLLKDR GITVEGTPAR TTAPAKARRL
ATTSSPPLAG LVERMLTNSD NDIGEALARQ TALATGEPAS FEGADRAVRK TLSKLNLPLT
GAVFADGSGL DRTDRASAGL LSRLLALATS AEHPELRSVA TGLPIAGFTG TLRGRYASEQ
AGAGTVRAKT GTLTGVNTLA GTVLDTDGRL LVFAFMTNHT TDAQAAQQAL DKMASALANC
GCR
//
