ID D1PM51_9FIRM Unreviewed; 405 AA.
AC D1PM51;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=SUBVAR_05409 {ECO:0000313|EMBL:EFB75636.1};
OS Subdoligranulum variabile DSM 15176.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Subdoligranulum.
OX NCBI_TaxID=411471 {ECO:0000313|EMBL:EFB75636.1, ECO:0000313|Proteomes:UP000003438};
RN [1] {ECO:0000313|EMBL:EFB75636.1, ECO:0000313|Proteomes:UP000003438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15176 {ECO:0000313|EMBL:EFB75636.1,
RC ECO:0000313|Proteomes:UP000003438};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (DEC-2009) 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:EFB75636.1}.
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DR EMBL; ACBY02000023; EFB75636.1; -; Genomic_DNA.
DR RefSeq; WP_007046796.1; NZ_GG704769.1.
DR AlphaFoldDB; D1PM51; -.
DR STRING; 411471.SUBVAR_05409; -.
DR MEROPS; S11.005; -.
DR GeneID; 78305625; -.
DR eggNOG; COG1686; Bacteria.
DR HOGENOM; CLU_027070_8_0_9; -.
DR OrthoDB; 9791132at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000003438; 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:SF34; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACC; 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:EFB75636.1}; 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:UP000003438};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..405
FT /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038474591"
FT DOMAIN 296..386
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00936"
FT ACT_SITE 82
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 85
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 142
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 246
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 405 AA; 43380 MW; A387C82E5FFA2613 CRC64;
MKKRTVTILL CLALVLFSVF RAYAEADSAV TVPAEVTPQA QTITPAGTSE FDVPCEAAIL
VDEDSGTVLY EKNADEQRPI ASITKVMTLL LTFQALESRK ISLEDNVPVS EHAYSMGGSQ
IWLEPGEQMT LNDMLKAICV SSANDAAVAV AEFVGGSEPA FVQMMNETAA QLGMTSTHFE
NACGLDQEGH LSSARDVAIM SREMLLHHTE VRDYCSIWTD TLRNGATQLV NTNKLLKSYN
GITGLKTGTT SKAGVCISAS AERNGLRLIA VVLGSASGKE RFQAATALLD YGFANFENIT
AELPDDAPQT IPVTRGTADA VALEYDTPQK CLVPKGQGEN LRIEVELPQT LQAPVKAGSQ
VGTVHWMDGE AELQTFTITA AQDVEALSFG YCFGLLVQSL ALSDV
//
