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Database: UniProt
Entry: U2FU55_9BURK
LinkDB: U2FU55_9BURK
Original site: U2FU55_9BURK 
ID   U2FU55_9BURK            Unreviewed;       299 AA.
AC   U2FU55;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, 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};
DE   AltName: Full=Penicillinase {ECO:0000256|ARBA:ARBA00030171};
GN   ORFNames=L810_3454 {ECO:0000313|EMBL:ERJ34080.1};
OS   Burkholderia sp. AU4i.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=1335308 {ECO:0000313|EMBL:ERJ34080.1, ECO:0000313|Proteomes:UP000016616};
RN   [1] {ECO:0000313|EMBL:ERJ34080.1, ECO:0000313|Proteomes:UP000016616}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU4i {ECO:0000313|EMBL:ERJ34080.1,
RC   ECO:0000313|Proteomes:UP000016616};
RA   Devi U., Khatri I., Kumar N., Kumar L., Singh D., Sharma D.,
RA   Subramanian S., Saini A.K.;
RT   "Genome Assembly of Burkholderia vietnamiensis AU4i.";
RL   Submitted (MAY-2013) 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:ERJ34080.1}.
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DR   EMBL; ASSI01000215; ERJ34080.1; -; Genomic_DNA.
DR   RefSeq; WP_021163199.1; NZ_ASSI01000215.1.
DR   AlphaFoldDB; U2FU55; -.
DR   PATRIC; fig|1335308.3.peg.7638; -.
DR   Proteomes; UP000016616; Unassembled WGS sequence.
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   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR   PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13354; Beta-lactamase2; 1.
DR   PRINTS; PR00118; BLACTAMASEA.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..299
FT                   /note="beta-lactamase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004627805"
FT   DOMAIN          56..268
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
SQ   SEQUENCE   299 AA;  31630 MW;  BE3D949D6D7886EE CRC64;
     MITRRQFTVT ALASAIAGVA AQAVCSAAHA QQGTVLASPF EMRLAQIEAQ VGGRLGVAIL
     DTASGKQVGW RMYERFPMCS TFKILLASLV LMRTDHGQED LTRKIVFSKR EVVPSSPVSG
     PRADSDGMTI AELCEAALTH SDNTAGNLLL TSVGGPTGLT AFARSIGDKF TRLDRNEPAL
     NEAAEGDPRD STTPAAILSD MHALLLGSTL SSSSRDQLIA WLVSNKTGDA RLRARLPKDW
     RIGDKTGTGD HGTVNDIAVV WPAGRAPVFV GAYLTGATNA TSTQRDEAIA KIGELVTEI
//
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