ID   A0A285JMK2_9ACTN        Unreviewed;       420 AA.
AC   A0A285JMK2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase (Penicillin-binding protein 5/6) {ECO:0000313|EMBL:SNY60566.1};
GN   ORFNames=SAMN05421748_121170 {ECO:0000313|EMBL:SNY60566.1};
OS   Actinoplanes atraurantiacus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=1036182 {ECO:0000313|EMBL:SNY60566.1, ECO:0000313|Proteomes:UP000219612};
RN   [1] {ECO:0000313|EMBL:SNY60566.1, ECO:0000313|Proteomes:UP000219612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.6857 {ECO:0000313|EMBL:SNY60566.1,
RC   ECO:0000313|Proteomes:UP000219612};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) 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; OBDY01000021; SNY60566.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285JMK2; -.
DR   Proteomes; UP000219612; 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:SNY60566.1};
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:SNY60566.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000219612};
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..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..420
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012651013"
FT   TRANSMEM        384..407
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          82..316
FT                   /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00768"
FT   REGION          349..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..377
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        116
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        119
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        173
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   BINDING         286
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ   SEQUENCE   420 AA;  42893 MW;  A7847CEF1FF01DC5 CRC64;
     MIRSILASLS AVALLIPVAA SPAEAAQAAA AAAPAIPCPK PKVAPPAGVP ARPVPPADDP
     VGFAIGGDAL ATHGLVIPAG VKQPPAVTAT TWMVADLDTG EVLGGCGPHV YQTPASVQKT
     LLAATAIGKL DPKKQITVTA DDLKIEPGSS AVGLVVGGKY TISTLWLGLL LNSGNDAANA
     LARLAGGGGK DGVAKTVAAM NDTARRLGAF QTHAVTPSGL DGKGQFTSAY DLALIARVCF
     ANADFRKYAL TKVAQMPAQP ALKKGGFQFQ NENKLIYKYP GALGGKTGFT QLARHSYVGA
     AQRNGRRLVV TLLGAEARPQ RGYDQGAALL DWGFSLPDDA SVGKLVTPEE TAAKSAAPSP
     IPEPATTGNQ AAAAADTRPT SPQLLSVAAA ASVALLLAAT PLLLLLTQRR RTRKPRKSRQ
//