ID D1LU76_PRORE Unreviewed; 261 AA.
AC D1LU76;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 2.
DT 27-MAR-2024, entry version 44.
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 Name=VEB-1 {ECO:0000313|EMBL:ACZ02434.2};
OS Providencia rettgeri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=587 {ECO:0000313|EMBL:ACZ02434.2};
RN [1] {ECO:0000313|EMBL:ACZ02434.2}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21609982; DOI=10.1093/jac/dkr197;
RA Aibinu I.E., Pfeifer Y., Ogunsola F., Odugbemi T., Koenig W.,
RA Ghebremedhin B.;
RT "Emergence of {beta}-lactamases OXA-10, VEB-1 and CMY in Providencia spp.
RT from Nigeria.";
RL J. Antimicrob. Chemother. 66:1931-1932(2011).
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; GU056840; ACZ02434.2; -; Genomic_DNA.
DR AlphaFoldDB; D1LU76; -.
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 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.
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 23..245
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACZ02434.2"
FT NON_TER 261
FT /evidence="ECO:0000313|EMBL:ACZ02434.2"
SQ SEQUENCE 261 AA; 29217 MW; 5C3E8E91A5B54B3F CRC64;
NLTLKIENVL KAKNARIGVA IFNSNEKDTL KINNDFHFPM QSVMKFPIAL AVLSEIDKGN
LSFEQKIEIT PQDLLPKTWS PIKEEFPNGT TLTIEQILNY TVSESDNIGC DILLKLIGGT
DSVQKFLNAN HFTDISIKAN EEQMHKDWNT QYQNWATPTA MNKLLIDTYN NKNQLLSKKS
YDFIWKIMRE TTTGSNRLKG QLPKNTIVAH KTGTSGINNG IAAATNDVGV ITLPNGQLIF
ISVFVAESKE TSEINEKIIS D
//