ID V5EES1_9LACO Unreviewed; 436 AA.
AC V5EES1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=Lc367_1356 {ECO:0000313|EMBL:EST03125.1};
OS Lactobacillus crispatus EM-LC1.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1328863 {ECO:0000313|EMBL:EST03125.1, ECO:0000313|Proteomes:UP000017999};
RN [1] {ECO:0000313|EMBL:EST03125.1, ECO:0000313|Proteomes:UP000017999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EM-LC1 {ECO:0000313|EMBL:EST03125.1,
RC ECO:0000313|Proteomes:UP000017999};
RX PubMed=24356836;
RA Power S.E., Harris H.M., Bottacini F., Ross R.P., O'Toole P.W.,
RA Fitzgerald G.F.;
RT "Draft Genome Sequence of Lactobacillus crispatus EM-LC1, an Isolate with
RT Antimicrobial Activity Cultured from an Elderly Subject.";
RL Genome Announc. 1:e01070-13(2013).
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:EST03125.1}.
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DR EMBL; AXLM01000036; EST03125.1; -; Genomic_DNA.
DR AlphaFoldDB; V5EES1; -.
DR MEROPS; S11.006; -.
DR PATRIC; fig|1328863.3.peg.1399; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000017999; 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:EST03125.1}; 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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..436
FT /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039615198"
FT DOMAIN 323..421
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00936"
FT ACT_SITE 79
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 82
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 143
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 436 AA; 47451 MW; 80DEF8DF598FE2A3 CRC64;
MDFMFFSKKI KRVAITTVAA VSIFSCGAVF ATTPVNADTT SSYQADQVKL NVKSAIAIDS
DSGQILYAKN AAQTLPIASM TKLVTVYLTL QAIKNHKLSW DQKVKPTAPI VKVANNAEYS
NVPLKLGHSY TIRQLYQATL IESANGAAML LGQTIAGSQK AFIDQMRAQV KKWGIEDAKI
YTACGLPNGN LGKDAYPGVN KNAENTMSAK DMAIVGQKLI SAFPEVLETT RLAHLNFKDA
GHVTKMANFN WMLKGLSQYD QAYPVDGLKT GTTDAAGACF IGTVQHNGAR LLTVVMGARH
RDGTDPARFE QTKKLMNYVF TKYRPVIMTA GSQMNGAKTI KVVDGDNATT NLGLKQKTTI
WDPADGKTLV ASLNKKSVEA PIKKDQTVGD YQFKSGNEKI VSLSNPNGMN VKAKALSANN
KVNFFVRIWR WIFGGR
//
