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Database: UniProt
Entry: D6D2E6_9BACE
LinkDB: D6D2E6_9BACE
Original site: D6D2E6_9BACE 
ID   D6D2E6_9BACE            Unreviewed;       293 AA.
AC   D6D2E6;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE            EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN   ORFNames=BXY_36210 {ECO:0000313|EMBL:CBK68598.1};
OS   Bacteroides xylanisolvens XB1A.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=657309 {ECO:0000313|EMBL:CBK68598.1, ECO:0000313|Proteomes:UP000008795};
RN   [1] {ECO:0000313|EMBL:CBK68598.1, ECO:0000313|Proteomes:UP000008795}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XB1A {ECO:0000313|EMBL:CBK68598.1,
RC   ECO:0000313|Proteomes:UP000008795};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Bernalier A.;
RT   "The genome sequence of Bacteriodes xylanisolvens XB1A.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBK68598.1, ECO:0000313|Proteomes:UP000008795}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XB1A {ECO:0000313|EMBL:CBK68598.1,
RC   ECO:0000313|Proteomes:UP000008795};
RA   Pajon A.;
RL   Submitted (MAR-2010) 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; FP929033; CBK68598.1; -; Genomic_DNA.
DR   AlphaFoldDB; D6D2E6; -.
DR   KEGG; bxy:BXY_36210; -.
DR   PATRIC; fig|657309.4.peg.2557; -.
DR   eggNOG; COG2367; Bacteria.
DR   HOGENOM; CLU_031960_0_1_10; -.
DR   Proteomes; UP000008795; Chromosome.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
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   Hydrolase {ECO:0000313|EMBL:CBK68598.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..293
FT                   /note="beta-lactamase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003082408"
FT   DOMAIN          44..265
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
SQ   SEQUENCE   293 AA;  32930 MW;  087A3240A3E37466 CRC64;
     MRSFIVFLCL VPTLLFARQT QLETQLKEAI KGKKAEIGIA VIIDGKDTVT VNNDIHYPLM
     SVFKFHQALA LADYMGKQKQ SLETRLPIKK SDLKPDTYSP LRDKYPQGEI EMSIADLLKY
     TLQQSDNNAC DILFDYQGGP DAVNKYIHSL GIRECAIAGT ETAMHEDLNL CYENWTTPLA
     AAELVEIFRK KPLFPNVYKD FIFQTMVECQ TGQDRLVAPL LDKKVTVGHK TGTGDLNAKG
     QQIGCNDIGF VLLPGGRTYS IAVFVKNSEE NNQVNSKIIA NISRIVYEYI MQH
//
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