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Database: UniProt
Entry: C3QTD3_9BACE
LinkDB: C3QTD3_9BACE
Original site: C3QTD3_9BACE 
ID   C3QTD3_9BACE            Unreviewed;       293 AA.
AC   C3QTD3;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE            EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN   ORFNames=BSCG_02142 {ECO:0000313|EMBL:EEO55217.1};
OS   Bacteroides sp. 2_2_4.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=469590 {ECO:0000313|EMBL:EEO55217.1};
RN   [1] {ECO:0000313|EMBL:EEO55217.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2_2_4 {ECO:0000313|EMBL:EEO55217.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA   Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA   Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA   White J., Yandava C., Allen-Vercoe E., Strauss J., Ambrose C., Lander E.,
RA   Nusbaum C., Ilzarbe M., Galagan J., Birren B.;
RT   "The Genome Sequence of Bacteroides sp. strain 2_2_4.";
RL   Submitted (DEC-2008) 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; EQ973358; EEO55217.1; -; Genomic_DNA.
DR   RefSeq; WP_008775626.1; NZ_EQ973358.1.
DR   AlphaFoldDB; C3QTD3; -.
DR   HOGENOM; CLU_031960_0_1_10; -.
DR   Proteomes; UP000003969; Unassembled WGS sequence.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:InterPro.
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   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_5002931450"
FT   DOMAIN          44..265
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
SQ   SEQUENCE   293 AA;  32832 MW;  AB0F57AF9ECE564B CRC64;
     MRSFIVFLCL VPTLLFARQT QLETQLKEAI KGKKAEIGIA VIIDGKDTVT VNNDIHYPLM
     SVFKFHQALA LADYMGKQRQ SLETQLPIKK SDLKPDTYSP LRDKYPQGGI EMSIADLLKY
     TLQQSDNNAC DILFDYQGGP DAVNKYIHSL GIRECAIAGT ETAMHEDLNL CYENWTTPLA
     AAELVEIFRK KPLFPKVYKD FIFQTMVECQ TGQDRLVAPL LDKKVTVGHK TGTGDLNAKG
     QQIGCNDIGF VLLPGGRTYS IAVFVKDSEE NNQANSKIIA DISRIVYEYV MQH
//
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