ID A0A071LV30_9ENTR Unreviewed; 402 AA.
AC A0A071LV30;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-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=DT73_09945 {ECO:0000313|EMBL:KEA52428.1};
OS Mangrovibacter sp. MFB070.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Mangrovibacter.
OX NCBI_TaxID=1224318 {ECO:0000313|EMBL:KEA52428.1, ECO:0000313|Proteomes:UP000027726};
RN [1] {ECO:0000313|EMBL:KEA52428.1, ECO:0000313|Proteomes:UP000027726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MFB070 {ECO:0000313|EMBL:KEA52428.1,
RC ECO:0000313|Proteomes:UP000027726};
RA Joseph T.C., Varghese A.M., Baby A., Reghunathan D., V M., Lalitha K.V.;
RT "Draft Genome Sequence of Mangrovibacter spp. MFB070 a Nitrogen-fixing
RT Bacterium Isolated from an Aquaculture Farm.";
RL Submitted (APR-2014) 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:KEA52428.1}.
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DR EMBL; JJMI01000022; KEA52428.1; -; Genomic_DNA.
DR RefSeq; WP_036107580.1; NZ_JJMI01000022.1.
DR AlphaFoldDB; A0A071LV30; -.
DR MEROPS; S11.003; -.
DR eggNOG; COG1686; Bacteria.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000027726; 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:SF6; TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 12; 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 Reference proteome {ECO:0000313|Proteomes:UP000027726};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..402
FT /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001679597"
FT DOMAIN 287..378
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00936"
FT ACT_SITE 68
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 71
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 134
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 402 AA; 43953 MW; 32FE8DAF4985E4C1 CRC64;
MNKRGLSSSF RAWCAGTTLL LLVSPQVFAE PAAPAAPAID AKAWILMDYA SGKVLAEGNA
DEKLDPASLT KLMTSYVVGQ ALKAGKIHLT DMVTVGDDAW ATGNPALRGS SVMFLKPRDR
VSVDDLNKGI VIQSGNDACI AMADYIAGSQ DAFVNLMNGY AKRLNLTNTT FKTVHGLDAP
GQFTTARDMA LLGQALVRDV PNEYAVNKEK EFTFNNIRQP NRNRLLWSSS LNVDGMKTGT
TAGAGYNLVA SATQGDMRLI SVVLGAKTDR IRFNESEKLL TWGFRFFETV TPISPDRPFV
TQRVWYGDNS EVNLGAGDAG AITIPRGQMK NLRASYTLNA PELTAPLKKG EVVGTINFQL
NGQTIEQRPL VVMEAVEEGG FFSRVWDYIQ FKFHQWFGGW FS
//