ID A0A0F9ZAJ6_9BACT Unreviewed; 307 AA.
AC A0A0F9ZAJ6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Peptidase S11 D-alanyl-D-alanine carboxypeptidase 1, D-alanyl-D-alanine carboxypeptidase (Penicillin-binding protein 5/6) {ECO:0000313|EMBL:KKP40789.1};
DE EC=3.4.16.4 {ECO:0000313|EMBL:KKP40789.1};
GN ORFNames=UR30_C0004G0047 {ECO:0000313|EMBL:KKP40789.1};
OS Candidatus Peregrinibacteria bacterium GW2011_GWC2_33_13.
OC Bacteria; Candidatus Peregrinibacteria.
OX NCBI_TaxID=1619061 {ECO:0000313|EMBL:KKP40789.1, ECO:0000313|Proteomes:UP000034765};
RN [1] {ECO:0000313|EMBL:KKP40789.1, ECO:0000313|Proteomes:UP000034765}
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:KKP40789.1}.
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DR EMBL; LBOR01000004; KKP40789.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F9ZAJ6; -.
DR STRING; 1619061.UR30_C0004G0047; -.
DR PATRIC; fig|1619061.3.peg.507; -.
DR Proteomes; UP000034765; 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-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR018044; Peptidase_S11.
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; 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:KKP40789.1};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KKP40789.1};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000313|EMBL:KKP40789.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..307
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002530509"
FT DOMAIN 56..286
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 93
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 96
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 148
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 307 AA; 33660 MW; EA40201293641E02 CRC64;
MLKALLSLIL LSGTAISNNL PANTETNILL TGKQMVIEEQ LKKKVLDITL PPGLKKKAAD
APLIQASSAL VYDLNSGVIL YQKNIDTKQP IASITKLMTA IIILEENDLN EIATIKQEST
QIGGVKIWLY TGEKITIANL LRGALIPSGN DAAHALAIHN SGSINLFVQK MNQKGQILGL
KNSHFANPMG FDDPENYSTA EDLVTLSKYA LKKKFIRDTV KISHTEVISE NGKIKHELSS
TNKLLTDSDI IVKGLKTGNT ENAGLCFIGL IQNTENHEFV SIVLNSPARF TETKTLSKWI
IDNYIWP
//
