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Database: UniProt
Entry: A0A235F4T3_9BACI
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ID   A0A235F4T3_9BACI        Unreviewed;       425 AA.
AC   A0A235F4T3;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
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   ORFNames=CGZ90_18615 {ECO:0000313|EMBL:OYD56242.1};
OS   Fictibacillus aquaticus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX   NCBI_TaxID=2021314 {ECO:0000313|EMBL:OYD56242.1, ECO:0000313|Proteomes:UP000215059};
RN   [1] {ECO:0000313|EMBL:OYD56242.1, ECO:0000313|Proteomes:UP000215059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GDSW-R2A3 {ECO:0000313|EMBL:OYD56242.1,
RC   ECO:0000313|Proteomes:UP000215059};
RA   Mayilraj S.;
RT   "Fictibacillus sp. nov. GDSW-R2A3 Genome sequencing and assembly.";
RL   Submitted (JUL-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   -!- 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}.
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:OYD56242.1}.
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DR   EMBL; NOII01000025; OYD56242.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A235F4T3; -.
DR   OrthoDB; 9791132at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000215059; Unassembled WGS sequence.
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:SF11; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACA; 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:OYD56242.1}; 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:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215059};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          283..395
FT                   /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00936"
FT   ACT_SITE        45
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        48
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        109
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   BINDING         233
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ   SEQUENCE   425 AA;  46895 MW;  A26CBDD66433AEEA CRC64;
     MFGFQSKASA APALDIKGEA AILIDGETGK ILFEKAADKM LPPASMTKMM TEYLVLEAIK
     KNKISWDQKT GISEHAHKIS QNRDLSNVPL RVDDKYSVKE LYQAMAIYSA NGATIALAEL
     IGGSESEFVS MMNKKAKQLG MKDFHFVNSS GLNNRDLRGE HPAGGENEEN MMSARSTAIL
     AFHLINDFPE VLETAKIPKL VFREGTDDKI NMENWNWMLP SLVYGYEGVD GLKTGSTDMA
     GFAFTGTVKK GDTRLLSVVM KTNSYKARFD ETAKLFNYGF ANFTKEKVLS KGYKIKGSKT
     LPVVKGKESE VAVAAKEDVS LVIKRGEKKN YKPKFVIDKK KLNEDGKLTA PIKKGDVVGH
     IQMEYKGEGE DYGYLINDGS GKGQVDVVTT KSVEKANWFV LAMRGIGSFF ADIWSGTVDM
     IKGLF
//
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