ID Q9RBQ1_STEMA Unreviewed; 303 AA.
AC Q9RBQ1;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 139.
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=blaL2 {ECO:0000313|EMBL:CAB63490.1};
GN Synonyms=L2 {ECO:0000313|EMBL:ABX44761.1};
OS Stenotrophomonas maltophilia (Pseudomonas maltophilia) (Xanthomonas
OS maltophilia).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=40324 {ECO:0000313|EMBL:CAB63490.1};
RN [1] {ECO:0000313|EMBL:CAB63490.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=K279a {ECO:0000313|EMBL:CAB63490.1};
RX PubMed=11158734; DOI=10.1128/AAC.45.2.413-419.2001;
RA Avison M.B., Higgins C.S., von Heldreich C.J., Bennett P.M., Walsh T.R.;
RT "Plasmid location and molecular heterogeneity of the L1 and L2 beta-
RT lactamase genes of Stenotrophomonas maltophilia.";
RL Antimicrob. Agents Chemother. 45:413-419(2001).
RN [2] {ECO:0000313|EMBL:CAD44949.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=405 {ECO:0000313|EMBL:CAD44949.1};
RA Petrella S., Pernot L.D., Sougakoff W.D.;
RT "Role of the disulfide bridge Cys69-Cys238 in class A beta-lactamases: a
RT structural and biochemical investigation in L2 from Stenotrophomonas
RT maltophilia.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007829|PDB:1O7E}
RP X-RAY CRYSTALLOGRAPHY (1.51 ANGSTROMS) OF 28-303.
RA Petrella S., Pernot L., Lascoux D., Forest E., Jarlier V., Sougakoff W.;
RT "Role of the Disulfide Bridge Cys69-Cys238 in Class a B-Lactamases : A
RT Structural and Biochemical Investigation on the B-Lactamase L2 from
RT Stenotrophomonas Maltophilia.";
RL Submitted (NOV-2002) to the PDB data bank.
RN [4] {ECO:0007829|PDB:1N4O}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 28-303.
RA Pernot L., Petrella S., Sougakoff W.;
RT "Role of the disulfide bridge Cys69-Cys238 in class A b-lactamases : a
RT structural and biochemical investigation on the b-lactamase L2 from
RT Stenotrophomonas maltophilia.";
RL Submitted (NOV-2002) to the PDB data bank.
RN [5] {ECO:0000313|EMBL:ABX44761.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KJ {ECO:0000313|EMBL:ABX44761.1};
RX PubMed=18086856; DOI=10.1128/AAC.00682-07;
RA Hu R.M., Huang K.J., Wu L.T., Hsiao Y.J., Yang T.C.;
RT "Induction of L1 and L2 beta-lactamases of Stenotrophomonas maltophilia.";
RL Antimicrob. Agents Chemother. 52:1198-1200(2008).
RN [6] {ECO:0000313|EMBL:ABX44761.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KJ {ECO:0000313|EMBL:ABX44761.1};
RA Hu R.-M., Huang K.-J., Hsiao Y.-J., Yang T.-C.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0007829|PDB:5NE1, ECO:0007829|PDB:5NE2}
RP X-RAY CRYSTALLOGRAPHY (1.19 ANGSTROMS) OF 28-303.
RX PubMed=28876489; DOI=10.1111/mmi.13831;
RA Calvopina K., Hinchliffe P., Brem J., Heesom K.J., Johnson S., Cain R.,
RA Lohans C.T., Fishwick C.W.G., Schofield C.J., Spencer J., Avison M.B.;
RT "Structural/mechanistic insights into the efficacy of nonclassical beta-
RT lactamase inhibitors against extensively drug resistant Stenotrophomonas
RT maltophilia clinical isolates.";
RL Mol. Microbiol. 106:492-504(2017).
RN [8] {ECO:0007829|PDB:6QW7}
RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 28-303.
RX PubMed=31383664; DOI=10.1128/AAC.00564-19;
RA Tooke C.L., Hinchliffe P., Lang P.A., Mulholland A.J., Brem J.,
RA Schofield C.J., Spencer J.;
RT "Molecular Basis of Class A beta-Lactamase Inhibition by Relebactam.";
RL Antimicrob. Agents Chemother. 63:e00564-e00519(2019).
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; EF601225; ABX44761.1; -; Genomic_DNA.
DR EMBL; AJ251816; CAB63490.1; -; Genomic_DNA.
DR EMBL; AJ506737; CAD44949.1; -; Genomic_DNA.
DR RefSeq; WP_076739548.1; NZ_JASJSS010000078.1.
DR PDB; 1N4O; X-ray; 1.85 A; A/B=28-303.
DR PDB; 1O7E; X-ray; 1.51 A; A/B=28-303.
DR PDB; 5NE1; X-ray; 2.09 A; A/B=28-303.
DR PDB; 5NE2; X-ray; 1.19 A; A/B=28-303.
DR PDB; 6QW7; X-ray; 1.78 A; A/B=28-303.
DR PDBsum; 1N4O; -.
DR PDBsum; 1O7E; -.
DR PDBsum; 5NE1; -.
DR PDBsum; 5NE2; -.
DR PDBsum; 6QW7; -.
DR AlphaFoldDB; Q9RBQ1; -.
DR SMR; Q9RBQ1; -.
DR BRENDA; 3.5.2.6; 5134.
DR EvolutionaryTrace; Q9RBQ1; -.
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; IPR049643; Beta-lactam_L2.
DR InterPro; IPR006311; TAT_signal.
DR NCBIfam; NF000232; lactamase_L2; 1.
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; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:1N4O, ECO:0007829|PDB:1O7E};
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..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..303
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011429318"
FT DOMAIN 59..275
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 303 AA; 31999 MW; BEFD3717C680EB73 CRC64;
MLARRRFLQF SGAAVASSLA LPLLARAAGK ATANAPTDAA ITAASDFAAL EKACAGRLGV
TLLDTASGRR IGHRQDERFP MCSTFKSMLA ATVLSQAERM PALLDRRVPV GEADLLSHAP
VTRRHAGKDM TVRDLCRATI ITSDNTAANL LFGVVGGPPA VTAFLRASGD TVSRSDRLEP
ELNSFAKGDP RDTTTPAAMA ATLQRVVLGE VLQPASRQQL ADWLIDNETG DACLRAGLGK
RWRVGDKTGS NGEDARNDIA VLWPVAGGAP WVLTAYLQAG AISYEQRASV LAQVGRIADR
LIG
//
