ID Q3SAW3_PSEAI Unreviewed; 283 AA.
AC Q3SAW3;
DT 11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2005, sequence version 1.
DT 27-MAR-2024, entry version 90.
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=bla(BEL1) {ECO:0000313|EMBL:AAZ04368.1};
GN Synonyms=blaBEL-1 {ECO:0000313|EMBL:ADB27941.1};
OS Pseudomonas aeruginosa.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=287 {ECO:0000313|EMBL:AAZ04368.1};
RN [1] {ECO:0000313|EMBL:AAZ04368.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=51170 {ECO:0000313|EMBL:AAZ04368.1};
RX PubMed=16127048; DOI=10.1128/AAC.49.9.3743-3748.2005;
RA Poirel L., Brinas L., Verlinde A., Ide L., Nordmann P.;
RT "BEL-1, a novel clavulanic acid-inhibited extended-spectrum beta-lactamase,
RT and the class 1 integron In120 in Pseudomonas aeruginosa.";
RL Antimicrob. Agents Chemother. 49:3743-3748(2005).
RN [2] {ECO:0000313|EMBL:ADB27941.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20200037; DOI=10.1093/jac/dkq048;
RA Glupczynski Y., Bogaerts P., Deplano A., Berhin C., Huang T.D.,
RA Van Eldere J., Rodriguez-Villalobos H.;
RT "Detection and characterization of class A extended-spectrum-beta-
RT lactamase-producing Pseudomonas aeruginosa isolates in Belgian hospitals.";
RL J. Antimicrob. Chemother. 65:866-871(2010).
RN [3] {ECO:0007829|PDB:5EOE, ECO:0007829|PDB:5EOO}
RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 19-283, AND DISULFIDE BONDS.
RX PubMed=27671060; DOI=10.1128/AAC.00936-16;
RA Pozzi C., De Luca F., Benvenuti M., Poirel L., Nordmann P., Rossolini G.M.,
RA Mangani S., Docquier J.D.;
RT "Crystal Structure of the Pseudomonas aeruginosa BEL-1 Extended-Spectrum
RT beta-Lactamase and Its Complexes with Moxalactam and Imipenem.";
RL Antimicrob. Agents Chemother. 60:7189-7199(2016).
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; DQ089809; AAZ04368.1; -; Genomic_DNA.
DR EMBL; GU250439; ADB27941.1; -; Genomic_DNA.
DR EMBL; GU250441; ADB27948.1; -; Genomic_DNA.
DR RefSeq; WP_063857830.1; NG_048704.1.
DR PDB; 5EOE; X-ray; 1.60 A; A/B=21-283.
DR PDB; 5EOO; X-ray; 1.48 A; A/B/C/D=19-283.
DR PDB; 5EPH; X-ray; 1.79 A; A/B/C/D=19-283.
DR PDB; 5EUA; X-ray; 1.85 A; A/B=19-283.
DR PDBsum; 5EOE; -.
DR PDBsum; 5EOO; -.
DR PDBsum; 5EPH; -.
DR PDBsum; 5EUA; -.
DR AlphaFoldDB; Q3SAW3; -.
DR SMR; Q3SAW3; -.
DR BindingDB; Q3SAW3; -.
DR ChEMBL; CHEMBL3885670; -.
DR KEGG; ag:AAZ04368; -.
DR BRENDA; 3.5.2.6; 5087.
DR SABIO-RK; Q3SAW3; -.
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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:5EOE, ECO:0007829|PDB:5EOO};
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..283
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009342754"
FT DOMAIN 50..256
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT DISULFID 61..231
FT /evidence="ECO:0007829|PDB:5EOE, ECO:0007829|PDB:5EOO"
SQ SEQUENCE 283 AA; 30945 MW; 4BB3FEDF4C4D8810 CRC64;
MKLLLYPLLL FLVIPAFAQA DFEHAISDLE AHNQAKIGVA LVSENGNLIQ GYRANERFAM
CSTFKLPLAA LVLSRIDAGE ENPERKLHYD SAFLEEYAPA AKRYVATGYM TVTEAIQSAL
QLSDNAAANL LLKEVGGPPL LTKYFRSLGD KVSRLDRIEP TLNTNTPGDE RDTTTPMSMA
QTVSKLIFGD TLTYKSKGQL RRLLIGNQTG DKTIRAGLPD SWVTGDKTGS CANGGRNDVA
FFITTAGKKY VLSVYTNAPE LQGEERALLI ASVAKLARQY VVH
//
