ID A0A0W7X5F6_9ACTN Unreviewed; 413 AA.
AC A0A0W7X5F6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:KUF17922.1};
GN ORFNames=AT728_10460 {ECO:0000313|EMBL:KUF17922.1};
OS Streptomyces silvensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1765722 {ECO:0000313|EMBL:KUF17922.1, ECO:0000313|Proteomes:UP000054804};
RN [1] {ECO:0000313|EMBL:KUF17922.1, ECO:0000313|Proteomes:UP000054804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53525 {ECO:0000313|EMBL:KUF17922.1,
RC ECO:0000313|Proteomes:UP000054804};
RA Johnston C.W., Li Y., Magarvey N.A.;
RT "Draft genome sequence of Streptomyces silvensis ATCC 53525, a producer of
RT novel hormone antagonists.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:KUF17922.1}.
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DR EMBL; LOCL01000033; KUF17922.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W7X5F6; -.
DR STRING; 1765722.AT728_10460; -.
DR Proteomes; UP000054804; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001967; Peptidase_S11_N.
DR PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR21581:SF33; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACB1; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000313|EMBL:KUF17922.1};
KW Hydrolase {ECO:0000313|EMBL:KUF17922.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:KUF17922.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054804};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..413
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006937086"
FT TRANSMEM 383..404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..311
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT REGION 22..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 413 AA; 43047 MW; 8594FE7A73DD4789 CRC64;
MPALKKTALL VASATLLSLS ATGPALADDK PGGKDDKPKP PASMSTVGGA RLGQPGTQVD
LKAGAPVLPK ELSARSWMVS DAETGEVLAA HNAHWRLAPA STLKMLFADT VLPKFPKTQQ
RKVQPADLAG IGAGSSLVGV KENETYSVHD LWLGVFLRSG NDAVHVLSAM NGGVPQTVKD
MQEHAEDLQA LDTRVVTPDG YDEKGQVSSA YDLTLFARSG LQKKDFREYC ATATAQFPGE
TKKIKKGKDK GKSKRESFGM QNTNRLLTGT DGVEQYKGIA GVKNGSTTNA GNTFTGVAER
DGKVLLVTVM NPGSDEPHAV YKESARLLDW GFAAADKVEP VGELVAPKGA KTGQGAPGKG
GQAGGAEGVA KATEKDSGSG SGMGTAFGIA AGVLAVIAGG LFLLNRRWPL RRQ
//
