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Database: UniProt
Entry: A0A1I6W9Y5_9BACI
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Original site: A0A1I6W9Y5_9BACI 
ID   A0A1I6W9Y5_9BACI        Unreviewed;       296 AA.
AC   A0A1I6W9Y5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=SAMN04488145_1262 {ECO:0000313|EMBL:SFT22803.1};
OS   Bacillus sp. 103mf.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1761751 {ECO:0000313|EMBL:SFT22803.1, ECO:0000313|Proteomes:UP000198993};
RN   [1] {ECO:0000313|EMBL:SFT22803.1, ECO:0000313|Proteomes:UP000198993}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=103MF {ECO:0000313|EMBL:SFT22803.1,
RC   ECO:0000313|Proteomes:UP000198993};
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|ARBA:ARBA00001526,
CC         ECO:0000256|RuleBase:RU361140};
CC   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000256|ARBA:ARBA00009009, ECO:0000256|RuleBase:RU361140}.
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DR   EMBL; FPAF01000026; SFT22803.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6W9Y5; -.
DR   STRING; 1761751.SAMN04488145_1262; -.
DR   Proteomes; UP000198993; Unassembled WGS sequence.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030655; P:beta-lactam 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; IPR045155; Beta-lactam_cat.
DR   InterPro; IPR000871; Beta-lactam_class-A.
DR   InterPro; IPR023650; Beta-lactam_class-A_AS.
DR   PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR   PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13354; Beta-lactamase2; 1.
DR   PRINTS; PR00118; BLACTAMASEA.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   PROSITE; PS00146; BETA_LACTAMASE_A; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251,
KW   ECO:0000256|RuleBase:RU361140};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361140};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          55..269
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
SQ   SEQUENCE   296 AA;  32369 MW;  546BDC1660F32E1E CRC64;
     MCVGILSLSL ASITLFTSEP LQVEAKEKTE QTKHTNHATH RELVQLEKKF DARIGVYAID
     TGTNRTVAYR PNERFAYAST FKALAAGAVL QQNSIDKLDE VITYTKDDLV TYSPITEKHV
     DTGMTLGEIA EAAICYSDNT AGNLLLKKLN GPNGFEKALR QIGDRVTMAD RFEPDLNEAT
     PGDIRDTSTP KALATNLKAF TIGNALPTDK RKILTDWMRG NTTGDQLIRA GVPKGWEVGD
     KSGAGSYGTR NDIAIVWPPN REPIIIAILS SRDTKDATYN NELIAQAAKI TINALK
//
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