ID   A0A1H0F6W7_9ACTN        Unreviewed;       770 AA.
AC   A0A1H0F6W7;
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 {ECO:0000313|EMBL:SDN90331.1};
GN   ORFNames=SAMN05216259_106177 {ECO:0000313|EMBL:SDN90331.1};
OS   Actinacidiphila guanduensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Actinacidiphila.
OX   NCBI_TaxID=310781 {ECO:0000313|EMBL:SDN90331.1, ECO:0000313|Proteomes:UP000199341};
RN   [1] {ECO:0000313|EMBL:SDN90331.1, ECO:0000313|Proteomes:UP000199341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.2022 {ECO:0000313|EMBL:SDN90331.1,
RC   ECO:0000313|Proteomes:UP000199341};
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; FNIE01000006; SDN90331.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0F6W7; -.
DR   STRING; 310781.SAMN05216259_106177; -.
DR   Proteomes; UP000199341; Unassembled WGS sequence.
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:SDN90331.1};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Protease {ECO:0000313|EMBL:SDN90331.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199341};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          442..644
FT                   /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00768"
FT   REGION          1..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          478..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..87
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        482..496
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        449
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        452
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        513
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   BINDING         613
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ   SEQUENCE   770 AA;  77703 MW;  65CCCFFFC6EEE8AA CRC64;
     MDAESASATP DVAPEAAPEP GPAPRGPKKP EPNRDHGGGA VEAPETPGAD GAGRPRTPAR
     TTPPREKQSR DDGSDGRKTE GETGEESGDA PSKSTAAAPR VAENGARTAG GQEGGTASAP
     AKGAEREAAK SGRAPEDEPG KAAAGAAGAA AVQDAKPAAG GKPARPAAKA DPQSAAKPAT
     KAADGRSEVF GGPGGPGPAE GADRAAEGAS AAAAADAPPA PAEPRRPVVK PLVSDLPPER
     PEEPPTRRLG AFRGSVAFGT PGKPTRADTG TSAPAPGTRS TAVPLPPEQP PAAGTASTAK
     APATPPAPEP AAAAGKAGAL PAEQDEVVGP EGTRGMPVPP VPDQAPLKLL AELTNTPPPP
     QTLVRTILRR VKIWTPLVVL LALVFVIVQA VRPLPSVSLA LTAAPSYTFA GTPLPDAMPW
     PTEGQSTAEV EGLGSLGVHG TQTPVPIASV TKVMTAYVVL QDHPISGKES GPKITVDAQA
     AQEAKSEDES HAPVKKGQQF TERQMLQLLL IPSGNNIARL LARWDAGTQD AFVAKMTAAA
     KRLGMTSTTY TGASGIEETT VSTAVDQLKL AQAVMKYDVF RSVVAQPNVD IPGVGRIFNN
     NNDLVNVGVV GIKTGSTTPA GGALMWAAHR TVAGKEQLIL GVVLEQHAGT TVDDSLQAAL
     QRSQRLIESV QGGLTSTTVV KKGEVIGHVS DGLGGSTPVV AAKDLTAIGW PGMKEQLSLT
     PAKDLPHSAK AGTQVGTLGF GSGSARTSVP VVLQSDLSEP GFGAKLTRLG
//