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Database: UniProt
Entry: A0A1G7IRN4_9BACL
LinkDB: A0A1G7IRN4_9BACL
Original site: A0A1G7IRN4_9BACL 
ID   A0A1G7IRN4_9BACL        Unreviewed;       368 AA.
AC   A0A1G7IRN4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE            EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN   ORFNames=SAMN04488542_106108 {ECO:0000313|EMBL:SDF15214.1};
OS   Fontibacillus panacisegetis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Fontibacillus.
OX   NCBI_TaxID=670482 {ECO:0000313|EMBL:SDF15214.1, ECO:0000313|Proteomes:UP000198972};
RN   [1] {ECO:0000313|EMBL:SDF15214.1, ECO:0000313|Proteomes:UP000198972}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28129 {ECO:0000313|EMBL:SDF15214.1,
RC   ECO:0000313|Proteomes:UP000198972};
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   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000256|ARBA:ARBA00009009}.
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DR   EMBL; FNBG01000006; SDF15214.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7IRN4; -.
DR   STRING; 670482.SAMN04488542_106108; -.
DR   Proteomes; UP000198972; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:InterPro.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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   PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR   PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13354; Beta-lactamase2; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW   Carboxypeptidase {ECO:0000313|EMBL:SDF15214.1};
KW   Hydrolase {ECO:0000313|EMBL:SDF15214.1};
KW   Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:SDF15214.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198972};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          59..288
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
SQ   SEQUENCE   368 AA;  41832 MW;  A3771D0EFB3CDAB0 CRC64;
     MIVLYIFMGI FALFLLLVLL LIVLKKINDK KTEQDVLKFI VKNPDRASFY VMENGKILVN
     TGAEIKRPLA SVVKIMVLAE FAEQVSAGMI DVAEEVHLSS LNRFYIPKTD GGAHSKWLDN
     LKEQGLDLEA KCTLKEVARG MILYSSNANT EFLIEKLGLE AINHRIQEWG LEQHDLIYPL
     SSSMLIPSYL MDTLDLSKKQ VAAYIADISY SDYANKASEI FNLLQSDEEG KWIDQLNRQE
     TSGLKLQELW SAKLPGSTVQ EYAHMLADIQ EGKLLSEQAQ PIFHELMEIK LKNPEPFIYV
     GQKGGSSISI INQVIYSEDM NGNKIQFALF IHDPFGADRI WLNKKFDLFI NKFFKDEPFK
     QQVVEALA
//
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