ID A0A073KIS8_9BACI Unreviewed; 369 AA.
AC A0A073KIS8;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN ORFNames=BAGA_20365 {ECO:0000313|EMBL:KEK22248.1};
OS Bacillus gaemokensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=574375 {ECO:0000313|EMBL:KEK22248.1, ECO:0000313|Proteomes:UP000027778};
RN [1] {ECO:0000313|EMBL:KEK22248.1, ECO:0000313|Proteomes:UP000027778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15801 {ECO:0000313|EMBL:KEK22248.1,
RC ECO:0000313|Proteomes:UP000027778};
RA Lai Q., Liu Y., Shao Z.;
RT "Draft genome sequence of Bacillus gaemokensis JCM 15801 (MCCC 1A00707).";
RL Submitted (JUN-2014) 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}.
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:KEK22248.1}.
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DR EMBL; JOTM01000036; KEK22248.1; -; Genomic_DNA.
DR RefSeq; WP_033677833.1; NZ_LTAQ01000056.1.
DR AlphaFoldDB; A0A073KIS8; -.
DR STRING; 574375.AZF08_13685; -.
DR eggNOG; COG2367; Bacteria.
DR OrthoDB; 975092at2; -.
DR Proteomes; UP000027778; Unassembled WGS sequence.
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:KEK22248.1};
KW Hydrolase {ECO:0000313|EMBL:KEK22248.1};
KW Protease {ECO:0000313|EMBL:KEK22248.1}.
FT DOMAIN 59..174
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 369 AA; 42263 MW; 4CEF01F32E4057C7 CRC64;
MRKGIVCAGI LGIFVLLISG NFLVGKVWSS NNDDAQYIAS YVEEHKDEKN SALLIKRNDK
VVYSVNPDIV LPVASTMKLI VAFEFAKQVT EGKIDPASFV SIDDVNRYYV PNADGGVQDR
WQRYLQRKGK IDENAVTLEE VAKGMMKFSS NTNTEYLMER LGLDNINQNL QSLSLPLHQP
LFPIVSSLYI PGYLHKELHV PKDKLEKKLK EMSPEQYRRY AMIIHDRLKE KGPLLQKEIP
LYFDGKYEKI WSDRLPAASA NDYMALLQKA NHKNGFTKLE KKEWANLVET DMSAKKYRKT
FRHAGQKNGY TPWTLAKAVY ATDKLGNCTE IVFLANHLDE DDSAELRKHL LNLHFQVLQS
DKYDATVIK
//
