ID A0A1I6RLL5_9BACL Unreviewed; 267 AA.
AC A0A1I6RLL5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
GN ORFNames=SAMN05428962_1923 {ECO:0000313|EMBL:SFS65599.1};
OS Paenibacillus sp. BC26.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1881032 {ECO:0000313|EMBL:SFS65599.1, ECO:0000313|Proteomes:UP000199637};
RN [1] {ECO:0000313|EMBL:SFS65599.1, ECO:0000313|Proteomes:UP000199637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC26 {ECO:0000313|EMBL:SFS65599.1,
RC ECO:0000313|Proteomes:UP000199637};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC ChEBI:CHEBI:140347; EC=3.5.2.6;
CC Evidence={ECO:0000256|RuleBase:RU361140};
CC -!- SIMILARITY: Belongs to the class-D beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00007898, ECO:0000256|RuleBase:RU361140}.
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DR EMBL; FPAD01000001; SFS65599.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6RLL5; -.
DR Proteomes; UP000199637; Unassembled WGS sequence.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0017001; P:antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR002137; Beta-lactam_class-D_AS.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR30627:SF6; BETA-LACTAMASE YBXI-RELATED; 1.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS00337; BETA_LACTAMASE_D; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|RuleBase:RU361140};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..267
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039529390"
FT DOMAIN 69..249
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT ACT_SITE 77
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR602137-50"
FT MOD_RES 80
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602137-50"
SQ SEQUENCE 267 AA; 30482 MW; 1264F5BEC87D2055 CRC64;
MITWRKKYRI WALSALLVAG TMGSASLPVN ATARDSKLQC ENLFHDVQGT LMIKNLKTDR
VYVCNPERSK QRFTPESSFK VPNALIGLEV KAVRDEYDVK RWDGVIRPFE AWNMDHSLAS
AMRASAIWYY QAMARDIGEE RMKNFVERIH YGNRDISGGI DTFWLNSSLK ISAEEQVGFM
EDLVKETLPF EEQTMKTVKR MMIDNDQDRY TVHGKTGTRL SDMGLGWYVG YVERGKTDFV
FVTNVDSSGS TAKTITLEAL TNLGIFK
//
