ID K2MMJ1_9BACI Unreviewed; 359 AA.
AC K2MMJ1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN ORFNames=BA1_05662 {ECO:0000313|EMBL:EKF36483.1};
OS Bacillus xiamenensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1178537 {ECO:0000313|EMBL:EKF36483.1, ECO:0000313|Proteomes:UP000010122};
RN [1] {ECO:0000313|EMBL:EKF36483.1, ECO:0000313|Proteomes:UP000010122}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HYC-10 {ECO:0000313|EMBL:EKF36483.1,
RC ECO:0000313|Proteomes:UP000010122};
RX PubMed=23209239; DOI=10.1128/JB.01920-12;
RA Lai Q., Liu Y., Shao Z.;
RT "Genome Sequence of Bacillus sp. Strain HYC-10, Isolated from Intestinal
RT Tract Contents from a Marine Fish (Mugil cephalus).";
RL J. Bacteriol. 194:6991-6991(2012).
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:EKF36483.1}.
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DR EMBL; AMSH01000009; EKF36483.1; -; Genomic_DNA.
DR RefSeq; WP_008356565.1; NZ_JAPDCO010000018.1.
DR AlphaFoldDB; K2MMJ1; -.
DR KEGG; bxi:BK049_07300; -.
DR PATRIC; fig|1178537.3.peg.1163; -.
DR eggNOG; COG2367; Bacteria.
DR Proteomes; UP000010122; 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:EKF36483.1};
KW Hydrolase {ECO:0000313|EMBL:EKF36483.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:EKF36483.1};
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 51..167
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 359 AA; 41123 MW; 0BD70C82B70A9EF7 CRC64;
MLLKIGLVVI GVVVLYVGVQ VLLYKRDMKK TKEDLLTFVA KNKKDVSVTI IENDDVMLEW
NADQKTPLAS TVKLVVLFHF VKAVSSGAIK LEEKVALPDI ERFYIDRTDG GAHAYWLEVN
DFSEHATLLD VAKGMMQFSS NACTDYLIDR LGLEKINDQM KQAGLTEPDE LMPLTPMILW
SAYVSDRRRD AFKKMSGVSE EQYKSLMNEI FNIMKNDPEH KKALEEKMKK KNLLGWRIQS
LLTQKLTKST TNQYAHFMKR LQDELLTIEE KSLFSQIVLG ETLKKETDQY LWYKGGATLF
VFTGALYRRT DTSSISISLF INDPKANNSH WIGGVFNEFM LTAAVDQNFR QRLIQAFTT
//
