ID   A0A1P8XVG1_9ACTN        Unreviewed;       540 AA.
AC   A0A1P8XVG1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:AQA12206.1};
GN   ORFNames=BV401_18870 {ECO:0000313|EMBL:AQA12206.1};
OS   Streptomyces autolyticus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=75293 {ECO:0000313|EMBL:AQA12206.1, ECO:0000313|Proteomes:UP000187851};
RN   [1] {ECO:0000313|Proteomes:UP000187851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC0516 {ECO:0000313|Proteomes:UP000187851};
RA   Yin M., Jiang M., Lu T.;
RT   "Streptomyces autolyticus CGMCC0516 complete genome sequence.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S13 family.
CC       {ECO:0000256|ARBA:ARBA00006096}.
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DR   EMBL; CP019458; AQA12206.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1P8XVG1; -.
DR   STRING; 75293.BV401_18870; -.
DR   KEGG; sauo:BV401_18870; -.
DR   OrthoDB; 9802627at2; -.
DR   Proteomes; UP000187851; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 1.
DR   PRINTS; PR00922; DADACBPTASE3.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:AQA12206.1};
KW   Hydrolase {ECO:0000313|EMBL:AQA12206.1};
KW   Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:AQA12206.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   540 AA;  56392 MW;  1A25EBBAF3C54AB0 CRC64;
     MSRPLNRRAH GWIWPLVIPL VIGLAFTLTW SSPAGADAGA DASGADTSRA GIGDALDTIL
     ADPLLKGGAA GVVVADADSG AVLYQHRPDD RLMPASNTKL FTSAAAMGLL GPGHRFRTDV
     LTDGSRNGRV LRGDLYLRGT GDPTMLAADY DRLAKDVADA GITRVTGRLI ADDTRFDAQR
     VGRSWAADDE SSYYAAQISA LTLAPDTDYD AGSVIVEVAP GAAAGDRPKV TVTPPNAYVR
     IDNRATTGGG TLTVERQHGS NTITVSGALP AGAATVKEWV SVWAPTGYAT SVFADALERH
     GVRVAGPTRL GRAAPADART LAAHRSMPLK ELLIPFMKLS NNIHAEALTK AIGHETAGRG
     TWDAGLAAIA DWLKKRGVDT GAVRQVDGSG LSRMDNIAAG RLTELLLSVR DEPWYADWYA
     SLPVACAPDR FVGGTLRTRM CSTPAAGNAR GKTGSLTGAS ALSGYVTDAD GRELVYSVVL
     NNYLASSVKN LEDAIVVTLA KSGEGHAEAV RPRAVRGDSA AKTATADAGL ECSWDKPRGC
//