ID A2WFY8_9BURK Unreviewed; 297 AA.
AC A2WFY8; A0A0D5IUY1;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
DE Flags: Fragment;
GN ORFNames=BDAG_03694 {ECO:0000313|EMBL:EAY70884.1};
OS Burkholderia dolosa AU0158.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=350701 {ECO:0000313|EMBL:EAY70884.1, ECO:0000313|Proteomes:UP000053482};
RN [1] {ECO:0000313|Proteomes:UP000053482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU0158 {ECO:0000313|Proteomes:UP000053482};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Devon K., Nusbaum C., Borowsky M.L.,
RA Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E., Brockman W., Rounsley S., Young S., LaButti K., Pushparaj V.,
RA DeCaprio D., Crawford M., Koehrsen M., Engels R., Montgomery P.,
RA Pearson M., Howarth C., Kodira C., Zeng Q., Yandava C., Oleary S.,
RA Alvarado L., Lory S., LiPuma J.;
RT "The Genome Sequence of Burkholderia dolosa (strain AU0158).";
RL Submitted (DEC-2005) 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 ECO:0000256|RuleBase:RU361140};
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00009009, ECO:0000256|RuleBase:RU361140}.
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DR EMBL; CH482381; EAY70884.1; -; Genomic_DNA.
DR RefSeq; WP_006766281.1; NZ_CP009793.1.
DR AlphaFoldDB; A2WFY8; -.
DR SMR; A2WFY8; -.
DR GeneID; 64457777; -.
DR PATRIC; fig|350701.8.peg.3923; -.
DR HOGENOM; CLU_031960_6_0_4; -.
DR OrthoDB; 9784149at2; -.
DR Proteomes; UP000053482; Unassembled WGS sequence.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
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; IPR023650; Beta-lactam_class-A_AS.
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; PS00146; BETA_LACTAMASE_A; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251,
KW ECO:0000256|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361140}.
FT DOMAIN 54..270
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT NON_TER 297
FT /evidence="ECO:0000313|EMBL:EAY70884.1"
SQ SEQUENCE 297 AA; 30991 MW; 54ABA161163027A3 CRC64;
MTHSSQRRTL LLAAAAAPLA LTVSACASSR GSTQDVASAT SFAALERAAG GRLGVCAIDT
ASGRRAQHRA DERFPFCSTF KAMLGAAVLA RSIAQPALLQ QRVAYGKADL VSYSPVTEQH
VGAGMTVAEL CAATIQYSDN TAANVLMKLI GGPQAVTAYA RSIGDATFRL DRWETELNTA
LPGDPRDTTT PAAMAASLRA LMLGDALPSA QRAQFVEWLR GNKVGDKRIR AGVPAGWRVG
DKTGTGDYGT TNDAGVAWPP SGAPIVLAVY YTQARADARA KDDVIAAATR IAVATLR
//
