ID R2P4F5_9ENTE Unreviewed; 430 AA.
AC R2P4F5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=UAK_02407 {ECO:0000313|EMBL:EOH78078.1};
OS Enterococcus raffinosus ATCC 49464.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1158602 {ECO:0000313|EMBL:EOH78078.1, ECO:0000313|Proteomes:UP000013877};
RN [1] {ECO:0000313|EMBL:EOH78078.1, ECO:0000313|Proteomes:UP000013877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49464 {ECO:0000313|EMBL:EOH78078.1,
RC ECO:0000313|Proteomes:UP000013877};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Enterococcus raffinosus ATCC_49464.";
RL Submitted (FEB-2013) 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:EOH78078.1}.
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DR EMBL; AJAL01000012; EOH78078.1; -; Genomic_DNA.
DR RefSeq; WP_010745621.1; NZ_KB946258.1.
DR AlphaFoldDB; R2P4F5; -.
DR GeneID; 67040795; -.
DR PATRIC; fig|1158602.3.peg.2408; -.
DR eggNOG; COG1686; Bacteria.
DR HOGENOM; CLU_027070_8_2_9; -.
DR OrthoDB; 9791132at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000013877; 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 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..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..430
FT /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004354020"
FT DOMAIN 306..414
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00936"
FT ACT_SITE 63
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 66
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 127
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 430 AA; 47525 MW; 031CC06C60948F10 CRC64;
MNKKKRFPFV LVVLVLFFQS LIGISARAAD DFSVNANAGY AIDADSGKVF FNQDGDTPKG
IASITKTITA YLVLDAIKQQ KITWEQEVPI SEYAEKLSTV PDLSNVTLVR GQKYTVKDLF
EAMIVQSANA CAVALAELIA GNEHTFVNQM REQLVKWDIK DATIINSSGL SNVYLGEHMY
PGTQENDENL MSARDVAIVA QHLIKDFPEV LETSKIKEKT FAPNTSQPDE MKNWNVMLFD
GPNYKEGVDG LKTGTTDLAG ACFVGTIQKD GRRVITVILN ALDQPNDENA RFAETSKLMD
YCLNNWSQQD VTVAGQTPTD KKELKVTEGK EKTVGLAMEK PVKLWVRNDM DPKNLTIKTT
LDQSLLDNNA VIAPVHKNEK LGTVSVSLTQ DTLGYVQANE AATTDLVTKN EVQKASTFEL
IWQKITGLFA
//
