ID H3SFJ8_9BACL Unreviewed; 409 AA.
AC H3SFJ8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=PDENDC454_11515 {ECO:0000313|EMBL:EHQ62227.1};
OS Paenibacillus dendritiformis C454.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1131935 {ECO:0000313|EMBL:EHQ62227.1, ECO:0000313|Proteomes:UP000003900};
RN [1] {ECO:0000313|EMBL:EHQ62227.1, ECO:0000313|Proteomes:UP000003900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C454 {ECO:0000313|EMBL:EHQ62227.1,
RC ECO:0000313|Proteomes:UP000003900};
RX PubMed=22461558; DOI=10.1128/JB.00158-12;
RA Sirota-Madi A., Olender T., Helman Y., Brainis I., Finkelshtein A.,
RA Roth D., Hagai E., Leshkowitz D., Brodsky L., Galatenko V., Nikolaev V.,
RA Gutnick D.L., Lancet D., Ben-Jacob E.;
RT "Genome Sequence of the Pattern-Forming Social Bacterium Paenibacillus
RT dendritiformis C454 Chiral Morphotype.";
RL J. Bacteriol. 194:2127-2128(2012).
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:EHQ62227.1}.
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DR EMBL; AHKH01000024; EHQ62227.1; -; Genomic_DNA.
DR RefSeq; WP_006676803.1; NZ_AHKH01000024.1.
DR AlphaFoldDB; H3SFJ8; -.
DR STRING; 1131935.PDENDC454_11515; -.
DR MEROPS; S11.005; -.
DR PATRIC; fig|1131935.3.peg.2372; -.
DR OrthoDB; 9791132at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000003900; 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:EHQ62227.1}; 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:UP000003900};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..409
FT /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003591392"
FT DOMAIN 300..391
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00936"
FT ACT_SITE 84
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 87
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 144
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 409 AA; 44849 MW; 4A87AB4878B247EF CRC64;
MKNRLYRVAC SALLSASLMT TGAAAAFADV PPWTGTEEPS QATSSTGAAE VQLAEHARSA
ILMDADTGTI IFQKNSHDRL PPASITKIMT MLLVMEAIDE GKLKPTDKVT TSEYAASMGG
SQIFLEPGEE MTVDEMMKGI AMASGNDASV AMAEKVAGSE KAFVQMMNEK AKELGMKDTH
FENSNGLPAD NHYTSAYDIA LMSQALLQYP GVTKYTGAYE DYLRQNTDKK FWLVNTNKLV
RFYQGADGLK TGYTSEAKFC LSATAKRDNL RVIAVVLGEP NTKTRNAEVT QMFDFTFAQY
MNVPILKKGD TIGSIRVEKG MVESLDLVAQ RPYHVLLKKG GSKDNVHFKL ESPESIKAPI
EKGQSLGKII VYQGDKAIRE YPVEATESVA KAGWWTLFKR TCGKLFFVK
//
