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Database: UniProt
Entry: A0A071LV30_9ENTR
LinkDB: A0A071LV30_9ENTR
Original site: A0A071LV30_9ENTR 
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
//
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