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Database: UniProt
Entry: V9W272_9BACL
LinkDB: V9W272_9BACL
Original site: V9W272_9BACL 
ID   V9W272_9BACL            Unreviewed;       392 AA.
AC   V9W272;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000256|ARBA:ARBA00012448};
DE            EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN   Name=dacF {ECO:0000313|EMBL:AHD05111.1};
GN   ORFNames=ERIC2_c12800 {ECO:0000313|EMBL:AHD05111.1};
OS   Paenibacillus larvae subsp. larvae DSM 25430.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=697284 {ECO:0000313|EMBL:AHD05111.1, ECO:0000313|Proteomes:UP000029431};
RN   [1] {ECO:0000313|EMBL:AHD05111.1, ECO:0000313|Proteomes:UP000029431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25430 {ECO:0000313|EMBL:AHD05111.1,
RC   ECO:0000313|Proteomes:UP000029431};
RX   PubMed=24599066;
RA   Djukic M., Brzuszkiewicz E., Funfhaus A., Voss J., Gollnow K., Poppinga L.,
RA   Liesegang H., Garcia-Gonzalez E., Genersch E., Daniel R.;
RT   "How to Kill the Honey Bee Larva: Genomic Potential and Virulence
RT   Mechanisms of Paenibacillus larvae.";
RL   PLoS ONE 9:E90914-E90914(2014).
CC   -!- FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell
CC       wall precursors. {ECO:0000256|ARBA:ARBA00003217}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC         transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC         substituents of D-alanine.; EC=3.4.16.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034000};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
CC   -!- SIMILARITY: Belongs to the peptidase S11 family.
CC       {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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DR   EMBL; CP003355; AHD05111.1; -; Genomic_DNA.
DR   RefSeq; WP_024093707.1; NZ_CP019652.1.
DR   AlphaFoldDB; V9W272; -.
DR   MEROPS; S11.005; -.
DR   GeneID; 64218300; -.
DR   KEGG; plv:ERIC2_c12800; -.
DR   PATRIC; fig|697284.3.peg.1213; -.
DR   eggNOG; COG1686; Bacteria.
DR   HOGENOM; CLU_027070_8_0_9; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000029431; Chromosome.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.410.10; D-Ala-D-Ala carboxypeptidase, C-terminal domain; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR015956; Peniciliin-bd_prot_C_sf.
DR   InterPro; IPR018044; Peptidase_S11.
DR   InterPro; IPR012907; Peptidase_S11_C.
DR   InterPro; IPR037167; Peptidase_S11_C_sf.
DR   InterPro; IPR001967; Peptidase_S11_N.
DR   PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR21581:SF6; TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 12; 1.
DR   Pfam; PF07943; PBP5_C; 1.
DR   Pfam; PF00768; Peptidase_S11; 1.
DR   PRINTS; PR00725; DADACBPTASE1.
DR   SMART; SM00936; PBP5_C; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF69189; Penicillin-binding protein associated domain; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW   ECO:0000313|EMBL:AHD05111.1}; Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AHD05111.1};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029431};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..392
FT                   /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5030179014"
FT   DOMAIN          283..374
FT                   /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00936"
FT   ACT_SITE        67
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        70
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        127
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   BINDING         233
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ   SEQUENCE   392 AA;  43514 MW;  C62629A63F3A06DE CRC64;
     MKTKWVTSLL LCSQLLFWTG FSYVHAEEKV PQQTDLTPNA KSAILLDADT GTIISEKDKD
     AKLPPASITK IMTMLLIMEA VDKGTLKMDE KVRTSEYAAS MGGSQIFLEP GEEMTVEEML
     KGIAMASGND ASVAMAEKIA GTEEDFVRMM NERAKQLGMK NTHFANCNGL PAENHYSTAY
     DIALMSRELL KHEKITAFTG AYQDYLRKDS EKPFWLVNTN KLVRFYNGAD GLKTGFTSEA
     KFCLAATAKR DNLRMIAVVM GEPDTKTRNA EVTKLFDYSF SQYTNYPIFK AGDQIGSFRV
     GKGKVQEVPL IAKHPYGVLL KKSEGKEGIR HEVQILPDLK APVQAGEPIG KLVVYKGDVK
     LKEFSLTSPV AVEKAGWWTI FKRGVGSLFQ TN
//
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