ID A2TJ38_SALTM Unreviewed; 299 AA.
AC A2TJ38;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 61.
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};
GN Name=blaPSE {ECO:0000313|EMBL:ABM92284.1};
OS Salmonella typhimurium.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90371 {ECO:0000313|EMBL:ABM92284.1};
RN [1] {ECO:0000313|EMBL:ABM92284.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=30/04 {ECO:0000313|EMBL:ABM92284.1};
RX PubMed=17419185;
RA Majtanova L., Majtan T., Majtan V.;
RT "Molecular characterization of class 1 integrons in clinical strains of
RT Salmonella typhimurium isolated in Slovakia.";
RL Pol. J. Microbiol. 56:19-23(2007).
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; EF204554; ABM92284.1; -; Genomic_DNA.
DR AlphaFoldDB; A2TJ38; -.
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};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..299
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002646537"
FT DOMAIN 52..268
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 299 AA; 32637 MW; 718D7E6AB45E680D CRC64;
MCDNQNYGVT YMKFLLAFSL LIPSVVFASS SKFQQVEQDV KAIEVSLSAR IGVSVLDTQN
GEYWDYNGNQ RFPLTSTFKT IACAKLLYDA EQGKVNPNST VEIKKADLVT YSPVIEKQVG
QAITLDDACF ATMTTSDNTA ANIILSAVGG PKGVTDFLRQ IGDKETRLDR IEPDLNEGKL
GDLRDTTTPK AIASTLNKFL FGSALSEMNQ KKLESWMVNN QVTGNLLRSV LPAGWNIADR
SGAGGFGARS ITAVVWSEHQ APIIVSIYLA QTQASMAERN DAIVKIGHSI FDVYTSQSR
//