ID Q82NJ2_STRAW Unreviewed; 388 AA.
AC Q82NJ2;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:BAC69021.1};
GN Name=dacA {ECO:0000313|EMBL:BAC69021.1};
GN ORFNames=SAVERM_1311 {ECO:0000313|EMBL:BAC69021.1};
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=227882 {ECO:0000313|EMBL:BAC69021.1, ECO:0000313|Proteomes:UP000000428};
RN [1] {ECO:0000313|EMBL:BAC69021.1, ECO:0000313|Proteomes:UP000000428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428};
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2] {ECO:0000313|EMBL:BAC69021.1, ECO:0000313|Proteomes:UP000000428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428};
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
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DR EMBL; BA000030; BAC69021.1; -; Genomic_DNA.
DR AlphaFoldDB; Q82NJ2; -.
DR KEGG; sma:SAVERM_1311; -.
DR eggNOG; COG1686; Bacteria.
DR HOGENOM; CLU_027070_3_1_11; -.
DR Proteomes; UP000000428; Chromosome.
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:BAC69021.1};
KW Hydrolase {ECO:0000313|EMBL:BAC69021.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:BAC69021.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000428};
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..388
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004300120"
FT TRANSMEM 357..378
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 67..298
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT REGION 40..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 388 AA; 39454 MW; F4AE71E4E242011A CRC64;
MSGMTIRFSS RMVGSCSALC VVGALALVPG PAVARTGVDP AAPKPTALQP PPLYRSGTQV
RPRAGAPEVP NVSALSWLVA DAGTGDVLAS HDAHRPLPPA STLKTLFALT MLPTLPGGIR
HTVAERELEG LGDGSSTVGV TEGQTYQVTD LWRGIFLHSG NDAVHVLASM NGGWDTTAHQ
MQAKARALGA LDTHVVSPDG YDAPGQTSSA YDLAIFGRAG LNREDFARYC STVDATFPGN
GGAYEIQNTN RLLTGADGIA PYPGLIGVKN GYTSNAGNTL VAAARRGGRT LVVTVLNPQS
GGGLAVYEEA RSLLDWGFGA AGRVDPVGSL LSARTVAQAG PATPDAVMAQ DGGGPGWPVT
GAIAGAAAVG AGAVVLALRF KGGRSGRR
//
