ID M3DCS3_9ACTN Unreviewed; 427 AA.
AC M3DCS3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:EMF27615.1};
GN ORFNames=H114_18231 {ECO:0000313|EMBL:EMF27615.1};
OS Streptomyces gancidicus BKS 13-15.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces pseudogriseolus group.
OX NCBI_TaxID=1284664 {ECO:0000313|EMBL:EMF27615.1, ECO:0000313|Proteomes:UP000011732};
RN [1] {ECO:0000313|EMBL:EMF27615.1, ECO:0000313|Proteomes:UP000011732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BKS 13-15 {ECO:0000313|EMBL:EMF27615.1,
RC ECO:0000313|Proteomes:UP000011732};
RX PubMed=23599292;
RA Kumar S., Kaur N., Singh N.K., Raghava G.P., Mayilraj S.;
RT "Draft Genome Sequence of Streptomyces gancidicus Strain BKS 13-15.";
RL Genome Announc. 1:E00150-13(2013).
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:EMF27615.1}.
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DR EMBL; AOHP01000073; EMF27615.1; -; Genomic_DNA.
DR AlphaFoldDB; M3DCS3; -.
DR PATRIC; fig|1284664.3.peg.3665; -.
DR Proteomes; UP000011732; 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:EMF27615.1};
KW Hydrolase {ECO:0000313|EMBL:EMF27615.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:EMF27615.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011732};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..427
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004032930"
FT TRANSMEM 390..412
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 78..314
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT REGION 33..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 427 AA; 44257 MW; 921E626DA62A255D CRC64;
MRTVPATEKT VRRSLLVASA VLLSTALTAP AALAAPSPST SPPAAPPAHT PVVGGERLGK
PGTQVNLAAG VPVLPKGLSG RSWIVADAET GDVLAAHDAH RPLAPASTLK MLFADTLLPK
WPRTTTHRVE PSDLAGVGAG SSMVGVKENE TYSVHDLWLG VFLRSGNDAV HVLAAMNGGV
DKTVDEMNAH AEELQALDTH AVSPDGYDAP GQVSSAYDLT LIARSGLQKK DFREYCSTVR
AQFPGETKKN KKGKRVRESF EIQNTNRLLS GDYDVPVYQG IAGVKNGNTT NAGATFTGVA
ERDGKVLLVT VMNPSKKESN EVYKETARLF DWGFAAAGKV EPVGELVPPK SVADATAAPG
PSASPGQAGG TGAGSQPVAS AHTGGGADGM GVALGITGGV LVLLAGGAFL VNRRWPLPDL
VRRRPRP
//
