ID   A0A1C5K3Z6_9ACTN        Unreviewed;       435 AA.
AC   A0A1C5K3Z6;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase (Penicillin-binding protein 5/6) {ECO:0000313|EMBL:SCG77249.1};
GN   ORFNames=GA0070613_6198 {ECO:0000313|EMBL:SCG77249.1};
OS   Micromonospora inositola.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=47865 {ECO:0000313|EMBL:SCG77249.1, ECO:0000313|Proteomes:UP000198221};
RN   [1] {ECO:0000313|EMBL:SCG77249.1, ECO:0000313|Proteomes:UP000198221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43819 {ECO:0000313|EMBL:SCG77249.1,
RC   ECO:0000313|Proteomes:UP000198221};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-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; LT607754; SCG77249.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C5K3Z6; -.
DR   Proteomes; UP000198221; Chromosome i.
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:SCG77249.1};
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:SCG77249.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198221};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          107..298
FT                   /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00768"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          410..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..27
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        113
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        116
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        180
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   BINDING         280
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ   SEQUENCE   435 AA;  45292 MW;  6A1BD6E02FD723AD CRC64;
     MYGEMRTVEF SRIPPAPPPA PPPPPVRRGR RRLPWVLSGL LALLLLGGAL YAVTPLRHPL
     PNPTVELTLP VSMTIPGTAP RLPWPRSGQA MISIDGLGTL GTSGGSKSLP IASVTKVMTA
     YVILTEHPLA VGAQGPKLTV SAEQAAAYPA EKARGESLVE VRAGEVITER QALQAVLLPS
     ANNMARILAA WDAGSVAAFV EKMNATADRL GMSGTHYTDP SGLDPDTVST ARDQVVLASK
     AMALPAFAEI VEQKQATLPV AGTVKNYNEL VGRNGVVGIK TGSTDEAGGC LVFAAVVNVG
     GRKLTIVGAV LGQPGADTPV QLDRVFAVTR SLLRSTVAAL AVHTLVEAGE QVATVRGPLG
     TGTTINAAEK VDVVGWPGLQ VRIDARIPAV PWRIAAGAEH GKLTVTAGGK PVGTALRTGT
     GMEPPSTWER IRHHR
//