ID   A0A1G7W7K1_9ACTN        Unreviewed;       369 AA.
AC   A0A1G7W7K1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase (Penicillin-binding protein 5/6) {ECO:0000313|EMBL:SDG67974.1};
GN   ORFNames=SAMN05421505_106235 {ECO:0000313|EMBL:SDG67974.1};
OS   Sinosporangium album.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Sinosporangium.
OX   NCBI_TaxID=504805 {ECO:0000313|EMBL:SDG67974.1, ECO:0000313|Proteomes:UP000198923};
RN   [1] {ECO:0000313|EMBL:SDG67974.1, ECO:0000313|Proteomes:UP000198923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CPCC 201354 {ECO:0000313|EMBL:SDG67974.1,
RC   ECO:0000313|Proteomes:UP000198923};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S11 family.
CC       {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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DR   EMBL; FNCN01000006; SDG67974.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7W7K1; -.
DR   STRING; 504805.SAMN05421505_106235; -.
DR   OrthoDB; 3663940at2; -.
DR   Proteomes; UP000198923; 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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR018044; Peptidase_S11.
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   PRINTS; PR00725; DADACBPTASE1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:SDG67974.1};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Protease {ECO:0000313|EMBL:SDG67974.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198923};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..369
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011678264"
FT   TRANSMEM        339..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          49..270
FT                   /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00768"
FT   REGION          300..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        83
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        86
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   BINDING         242
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ   SEQUENCE   369 AA;  38153 MW;  671232D22E6E70D5 CRC64;
     MGTKHLVSVT ALLASVVLVH APPAQARTAP PIGGDLLGHR GLVAPAEVKA PPKTKARSYV
     VADAGTGEVL AAKDAHGRYL PASTLKSLTA LTLIPQLNRN KRVTPSRTAC NQEGSAVGLV
     PKPLYQVHDL FRALMLSSGN DAAMALAEAN GGLEPTLAQM NAVAHKLQAM DTVAKTPSGL
     DKAGQSSSAY DLALITRAGL ANPEFRRYVS TKTAKFPAPK GYYEIGNHNK LLWSYDGMVG
     GKNGWTTKAM GSFSGAATRG GHTVIVAIMR HEGAFWGEVA DLLDWGFAAR GKVTPVGRLV
     DPLPDKPAQT ASPSPVGTPM NAAPADAAKA SAPGTGSGLA VPLLIGVSLL GGVAGVLYGM
     RRKVKARAR
//