ID A0A0S7YEJ5_9BACT Unreviewed; 298 AA.
AC A0A0S7YEJ5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Peptidase S11 D-alanyl-D-alanine carboxypeptidase A N-terminal domain-containing protein {ECO:0000259|Pfam:PF00768};
GN ORFNames=AMJ48_02885 {ECO:0000313|EMBL:KPJ72947.1};
OS Parcubacteria bacterium DG_74_1.
OC Bacteria; Candidatus Parcubacteria.
OX NCBI_TaxID=1703765 {ECO:0000313|EMBL:KPJ72947.1, ECO:0000313|Proteomes:UP000051540};
RN [1] {ECO:0000313|EMBL:KPJ72947.1, ECO:0000313|Proteomes:UP000051540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_74_1 {ECO:0000313|EMBL:KPJ72947.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(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:KPJ72947.1}.
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DR EMBL; LJNE01000010; KPJ72947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7YEJ5; -.
DR STRING; 1703765.AMJ48_02885; -.
DR Proteomes; UP000051540; 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 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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..298
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006640614"
FT DOMAIN 56..275
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 90
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 93
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 145
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 248
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 298 AA; 33698 MW; E4E13965BC554B83 CRC64;
MKSKIFFFLL LLLFLFSPAI AKGAKISQEQ ILQRVEIIQQ EMKLLKSLLS GMQAANQGAR
ISARSYLAVN LSDNSILLKQ NINRRYPIAS ITKLMTAVIA FEELDLDQKI TLTKEMLEPD
GYSPSLYLGL SIDAEELVKA SLIQSTNDAA EALSYFMKKD KFVALMNQKA KELKMTNTVF
YDPHGLNPDN QSTVQDLTKL LIYIYKNHPE ILDITRNNNF WLPDSTGRLL KFRNLNSFYP
LSSFIGGKVG YLFEARQTFA SLFNIKGDTV AVVILYSDNH RADIFAILKS SKQSLSSR
//
