ID   A0A265NFL3_9BACI        Unreviewed;       370 AA.
AC   A0A265NFL3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:OZU90066.1};
GN   ORFNames=CIL03_02705 {ECO:0000313|EMBL:OZU90066.1};
OS   Virgibacillus indicus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX   NCBI_TaxID=2024554 {ECO:0000313|EMBL:OZU90066.1, ECO:0000313|Proteomes:UP000216498};
RN   [1] {ECO:0000313|EMBL:OZU90066.1, ECO:0000313|Proteomes:UP000216498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IO3-P2-C2 {ECO:0000313|EMBL:OZU90066.1,
RC   ECO:0000313|Proteomes:UP000216498};
RA   Xu B., Hu B., Wang J., Zhu Y., Huang L., Du W., Huang Y.;
RT   "Virgibacillus indicus sp. nov. and Virgibacillus profoundi sp. nov, two
RT   moderately halophilic bacteria isolated from marine sediment by using the
RT   Microfluidic Streak Plate.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell
CC       wall precursors. {ECO:0000256|ARBA:ARBA00003217}.
CC   -!- SIMILARITY: Belongs to the peptidase S11 family.
CC       {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OZU90066.1}.
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DR   EMBL; NPMS01000001; OZU90066.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A265NFL3; -.
DR   OrthoDB; 9791132at2; -.
DR   Proteomes; UP000216498; 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; 2.30.140.30; -; 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; IPR001967; Peptidase_S11_N.
DR   PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR21581:SF32; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACB; 1.
DR   Pfam; PF00768; Peptidase_S11; 1.
DR   PRINTS; PR00725; DADACBPTASE1.
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:0000313|EMBL:OZU90066.1};
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:OZU90066.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216498};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          23..246
FT                   /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00768"
FT   ACT_SITE        57
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        60
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        112
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   BINDING         216
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ   SEQUENCE   370 AA;  41439 MW;  A164531558F158A9 CRC64;
     MRFISLVLLF FIFFSFTGPV TGQAKPGVSA HNAILIEQST GRVLYEKNGN DMESIASITK
     VMTAILAIES GKMNEKAAAS RKAIYTEGSS IYLEQGEKML IEDLVYGLML RSGNDAAIAI
     SEHIGGSEEG FVHLMNEKAR WLGMTNTNFD NPHGLDSDNH YSSAYDMALL MRYAMQDEEF
     RKVTGTTTYK SENRSYSWQN KNKLLTQLYE SCTGGKTGYT KKTGRTLISS ASKNGMDLIA
     VTLNAPDDWN DHISMYEWGF ENYEMETIIE KGEFQYIPKG SDGTQTGFIH NDIFYPLQGN
     EITNVDKKAY LLKKKHDAPS DIIGKTVFYL NDIPISEVLI YSGQDNGKKQ GFISEILSIY
     QKIIGLKNYG
//