ID Q4PKA5_9BACT Unreviewed; 380 AA.
AC Q4PKA5;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000256|ARBA:ARBA00012448};
DE EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
OS uncultured bacterium MedeBAC35C06.
OC Bacteria; environmental samples.
OX NCBI_TaxID=332273 {ECO:0000313|EMBL:AAY82600.1};
RN [1] {ECO:0000313|EMBL:AAY82600.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16008504; DOI=10.1371/journal.pbio.0030273;
RA Sabehi G., Loy A., Jung K.H., Partha R., Spudich J.L., Isaacson T.,
RA Hirschberg J., Wagner M., Beja O.;
RT "New insights into metabolic properties of marine bacteria encoding
RT proteorhodopsins.";
RL PLoS Biol. 3:E273-E273(2005).
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; DQ077553; AAY82600.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4PKA5; -.
DR UniPathway; UPA00219; -.
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 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}.
FT DOMAIN 269..359
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00936"
FT ACT_SITE 57
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 60
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 117
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 380 AA; 42029 MW; 8CAF9A306E2A34AB CRC64;
MKKLLTLLLF TSCLELYSQS FVAPAPKLDL KAYILIEPQT GTVIAEYNSD LHVEPASMTK
IMTGYVVADQ IGNDLINLND SVLISERAWR MGGSKMFIEA GKRVSVEDLL KGVIIQSGND
ASVALAEYSG GTEEGFVDLM NAYAQSLGMN NTTFLNSTGL PAEGHYSSAK DLAYLTSNFI
NKFPEIYSLY KEKSFEFNSI KQLNRNKLLW RDDSSDGVKT GHTESAGYCL VGSAKRGGMR
LITVVAGSSS DKKRFDDTQR LLEYGFRFFS TQEVLKKDQV YKTVKVWGGQ KSEAGLGVAA
NQILTLPRVD FKDLQINYIY KNNIQAPIKK GDVIGSIEII SNDSPVLVTD LVALDQVEAK
GFFGRLWSKF ILWIMSLFGG
//
