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Database: UniProt
Entry: A0A0U5JI58_9CLOT
LinkDB: A0A0U5JI58_9CLOT
Original site: A0A0U5JI58_9CLOT 
ID   A0A0U5JI58_9CLOT        Unreviewed;       419 AA.
AC   A0A0U5JI58;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000256|ARBA:ARBA00012448};
DE            EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
DE   Flags: Precursor;
GN   Name=dacF {ECO:0000313|EMBL:CUX43604.1};
GN   ORFNames=BN3456_02351 {ECO:0000313|EMBL:CUX43604.1};
OS   Clostridium sp. C105KSO13.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1776045 {ECO:0000313|EMBL:CUX43604.1, ECO:0000313|Proteomes:UP000198973};
RN   [1] {ECO:0000313|EMBL:CUX43604.1, ECO:0000313|Proteomes:UP000198973}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C105KSO131 {ECO:0000313|EMBL:CUX43604.1};
RA   McClelland M., Jain A., Saraogi P., Mendelson R., Westerman R.,
RA   SanMiguel P., Csonka L.;
RL   Submitted (JAN-2016) 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}.
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DR   EMBL; FBWL01000169; CUX43604.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0U5JI58; -.
DR   STRING; 1776045.BN3456_02351; -.
DR   OrthoDB; 9791132at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000198973; 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: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:CUX43604.1}; Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CUX43604.1};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198973};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..419
FT                   /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006860497"
FT   DOMAIN          314..401
FT                   /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00936"
FT   REGION          30..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..50
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        91
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        94
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        151
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   BINDING         261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ   SEQUENCE   419 AA;  45633 MW;  D4928A86B5F98B1B CRC64;
     MKRVLAVLLS TFLCLQNVYA MPAKEHIVYE DTQENIENTE DTENKDDSEG EQPAEEAAGP
     QVSAPSAVLM EASTGEVICE KDADTPRPPA SVTKVMTMLL IFDALAEGKI KLEDQVTTSE
     YAASMGGSQV FLEAGETQTV DTMLKCISVA SGNDACVAMA EYICGNEEEF VRQMNEKAKS
     LGMENTHFVN CNGLDADGHV TTARDIALMS RELITKYPQI QDYCMIWMEN ITHTTQKGTS
     EFGLTNTNKL VRQYEYATGL KTGSTGLAKF CVSATAKKND VDLIAVIMAA EDSKARFKDA
     TTLLNYGFGK CQVYKDEKPQ KLKDIVVDGG VEDTVPCKYS GTFRYLDTTG ANLAGITKKL
     NMKKSLDAPV RKGDAAGSLV YELDGKEIGK VDVIASKNVK KAGIFDYLKK VMKSFSIAA
//
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