ID A0A0G0RXQ8_9BACT Unreviewed; 299 AA.
AC A0A0G0RXQ8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:KKR54721.1};
GN ORFNames=UT91_C0010G0014 {ECO:0000313|EMBL:KKR54721.1};
OS Parcubacteria group bacterium GW2011_GWA2_40_23.
OC Bacteria.
OX NCBI_TaxID=1618816 {ECO:0000313|EMBL:KKR54721.1, ECO:0000313|Proteomes:UP000034534};
RN [1] {ECO:0000313|EMBL:KKR54721.1, ECO:0000313|Proteomes:UP000034534}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKR54721.1}.
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DR EMBL; LBYP01000010; KKR54721.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0RXQ8; -.
DR STRING; 1618816.UT91_C0010G0014; -.
DR PATRIC; fig|1618816.3.peg.698; -.
DR Proteomes; UP000034534; Unassembled WGS sequence.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:InterPro.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000871; Beta-lactam_class-A.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR001967; Peptidase_S11_N.
DR PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:KKR54721.1};
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:0000313|EMBL:KKR54721.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..299
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002534317"
FT DOMAIN 48..276
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 78
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 81
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 133
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 246
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 299 AA; 33637 MW; 2E31D9CE865406D9 CRC64;
MLTNLLLVLL FLNPFSSAYP TDRDFFNVAQ VSSVSAPSRI NPENVGLEAT AEKYVAIDVI
SGKILIQKNV DSVQPIASIT KLMTALVVLD NVKDWDKTVE MNRVDETYGA FAHIYRGEEV
SFEDLWNAAL ISSDNNSIMA MIRALGFSQE EFVTKMNIKA KELQMYNTSF SDPTGLSVEN
QSTALDISRL LYTALNQAKI QSTVTKNKYT FKVLNNSKTR TVTSTDILLD SFLNRKQYGY
QLVGGKTGYI PEAGYCLTVE IEKEKHSVII TVLNSNNIEN RFQDVKVIAD WVFNNYSWE
//
