BLA1_STEMA
ID BLA1_STEMA Reviewed; 290 AA.
AC P52700;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Metallo-beta-lactamase L1 type 3 {ECO:0000305};
DE EC=3.5.2.6 {ECO:0000269|PubMed:3931629};
DE AltName: Full=B3 metallo-beta-lactamase {ECO:0000305};
DE AltName: Full=Beta-lactamase type III {ECO:0000303|PubMed:3931629};
DE AltName: Full=Metallo-beta-lactamase L1 type III {ECO:0000303|PubMed:3931629};
DE AltName: Full=Penicillinase {ECO:0000303|PubMed:3931629};
DE Flags: Precursor;
OS Stenotrophomonas maltophilia (Pseudomonas maltophilia) (Xanthomonas
OS maltophilia).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=40324;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IID 1275;
RX PubMed=8018721; DOI=10.1016/0167-4781(94)90011-6;
RA Walsh T.R., Hall L., Assinder S.J., Nichols W.W., Cartwright S.J.,
RA Macgowan A.P., Bennett P.M.;
RT "Sequence analysis of the L1 metallo-beta-lactamase from Xanthomonas
RT maltophilia.";
RL Biochim. Biophys. Acta 1218:199-201(1994).
RN [2]
RP PROTEIN SEQUENCE OF 34-65, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=IID 1275;
RX PubMed=3931629; DOI=10.1042/bj2290791;
RA Bicknell R., Emanuel E.L., Gagnon J., Waley S.G.;
RT "The production and molecular properties of the zinc beta-lactamase of
RT Pseudomonas maltophilia IID 1275.";
RL Biochem. J. 229:791-797(1985).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 22-290 IN COMPLEX WITH ZINC IONS,
RP FUNCTION, COFACTOR, SUBUNIT, DISULFIDE BOND, AND REACTION MECHANISM.
RX PubMed=9811546; DOI=10.1006/jmbi.1998.2148;
RA Ullah J.H., Walsh T.R., Taylor I.A., Emery D.C., Verma C.S., Gamblin S.J.,
RA Spencer J.;
RT "The crystal structure of the L1 metallo-beta-lactamase from
RT Stenotrophomonas maltophilia at 1.7 A resolution.";
RL J. Mol. Biol. 284:125-136(1998).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 22-290 IN COMPLEX WITH SUBSTRATE
RP ANALOGS AND ZINC, COFACTOR, AND SUBUNIT.
RX PubMed=17999929; DOI=10.1016/j.jmb.2007.10.036;
RA Nauton L., Kahn R., Garau G., Hernandez J.F., Dideberg O.;
RT "Structural insights into the design of inhibitors for the L1 metallo-beta-
RT lactamase from Stenotrophomonas maltophilia.";
RL J. Mol. Biol. 375:257-269(2008).
CC -!- FUNCTION: Confers resistance to the different beta-lactams antibiotics
CC (penicillin, cephalosporin and carbapenem) via the hydrolysis of the
CC beta-lactam ring. {ECO:0000269|PubMed:3931629,
CC ECO:0000269|PubMed:9811546}.
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:0000269|PubMed:3931629};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:17999929, ECO:0000269|PubMed:9811546};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:17999929,
CC ECO:0000269|PubMed:9811546};
CC -!- ACTIVITY REGULATION: Inhibited by Hg(2+) or Cu(2+), and by chelating
CC agents such as EDTA and O-phenanthroline. Reduced enzymatic activity in
CC presence of cobalt, nickel, cadmium, and manganese.
CC {ECO:0000269|PubMed:3931629}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Unstable below pH 8, unless zinc is present.
CC {ECO:0000269|PubMed:3931629};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17999929,
CC ECO:0000269|PubMed:3931629, ECO:0000269|PubMed:9811546}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. Class-B
CC beta-lactamase family. {ECO:0000305}.
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DR EMBL; X75074; CAA52968.1; -; Genomic_DNA.
DR PIR; S45349; S45349.
DR PDB; 1SML; X-ray; 1.70 A; A=22-290.
DR PDB; 2AIO; X-ray; 1.70 A; A=22-290.
DR PDB; 2FM6; X-ray; 1.75 A; A/B=22-290.
DR PDB; 2FU6; X-ray; 2.05 A; A/B=22-290.
DR PDB; 2FU7; X-ray; 1.85 A; A/B=22-290.
DR PDB; 2FU8; X-ray; 1.80 A; A/B=22-290.
DR PDB; 2FU9; X-ray; 1.80 A; A/B=22-290.
DR PDB; 2GFJ; X-ray; 1.80 A; A/B=22-290.
DR PDB; 2GFK; X-ray; 1.90 A; A/B=22-290.
DR PDB; 2H6A; X-ray; 1.80 A; A/B=22-290.
DR PDB; 2HB9; X-ray; 1.75 A; A=22-290.
DR PDB; 2QDT; X-ray; 2.00 A; A=22-290.
DR PDB; 2QIN; X-ray; 1.76 A; A/B/C/D=22-290.
DR PDB; 2QJS; X-ray; 2.25 A; A/B/C/D=22-290.
DR PDB; 5DPX; X-ray; 1.85 A; A/B=22-290.
DR PDB; 5EVB; X-ray; 1.84 A; A=22-290.
DR PDB; 5EVD; X-ray; 1.80 A; A=22-290.
DR PDB; 5EVK; X-ray; 1.63 A; A=22-290.
DR PDB; 5HH5; X-ray; 1.80 A; A=22-290.
DR PDB; 5HH6; X-ray; 1.80 A; A=22-290.
DR PDB; 7A63; X-ray; 1.57 A; A=22-290.
DR PDB; 7AFZ; X-ray; 1.50 A; A=22-290.
DR PDB; 7BJ8; X-ray; 1.69 A; A=22-290.
DR PDB; 7O0O; X-ray; 1.45 A; A=22-290.
DR PDBsum; 1SML; -.
DR PDBsum; 2AIO; -.
DR PDBsum; 2FM6; -.
DR PDBsum; 2FU6; -.
DR PDBsum; 2FU7; -.
DR PDBsum; 2FU8; -.
DR PDBsum; 2FU9; -.
DR PDBsum; 2GFJ; -.
DR PDBsum; 2GFK; -.
DR PDBsum; 2H6A; -.
DR PDBsum; 2HB9; -.
DR PDBsum; 2QDT; -.
DR PDBsum; 2QIN; -.
DR PDBsum; 2QJS; -.
DR PDBsum; 5DPX; -.
DR PDBsum; 5EVB; -.
DR PDBsum; 5EVD; -.
DR PDBsum; 5EVK; -.
DR PDBsum; 5HH5; -.
DR PDBsum; 5HH6; -.
DR PDBsum; 7A63; -.
DR PDBsum; 7AFZ; -.
DR PDBsum; 7BJ8; -.
DR PDBsum; 7O0O; -.
DR AlphaFoldDB; P52700; -.
DR SMR; P52700; -.
DR BindingDB; P52700; -.
DR ChEMBL; CHEMBL3326; -.
DR DrugBank; DB02365; 1,10-Phenanthroline.
DR DrugBank; DB08702; 2,5-DIPHENYLFURAN-3,4-DICARBOXYLIC ACID.
DR DrugBank; DB08069; 4-AMINO-5-(2-METHYLPHENYL)-2,4-DIHYDRO-3H-1,2,4-TRIAZOLE-3-THIONE.
DR DrugBank; DB02032; Epicaptopril.
DR DrugBank; DB04740; Moxalactam (hydrolyzed).
DR DrugBank; DB07939; N-(3-MERCAPTOPROPANOYL)-D-ALANINE.
DR DrugBank; DB08199; N-[(BENZYLOXY)CARBONYL]-L-CYSTEINYLGLYCINE.
DR BRENDA; 3.5.2.6; 5134.
DR SABIO-RK; P52700; -.
DR EvolutionaryTrace; P52700; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0008800; F:beta-lactamase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0017001; P:antibiotic catabolic process; IDA:UniProtKB.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR001018; Beta-lactamase_class-B_CS.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR PROSITE; PS00743; BETA_LACTAMASE_B_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Direct protein sequencing;
KW Disulfide bond; Hydrolase; Metal-binding; Periplasm; Signal; Zinc.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..33
FT /evidence="ECO:0000269|PubMed:3931629"
FT /id="PRO_0000016947"
FT CHAIN 34..290
FT /note="Metallo-beta-lactamase L1 type 3"
FT /id="PRO_0000016948"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17999929,
FT ECO:0000269|PubMed:9811546"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17999929,
FT ECO:0000269|PubMed:9811546"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17999929,
FT ECO:0000269|PubMed:9811546"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17999929,
FT ECO:0000269|PubMed:9811546"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17999929,
FT ECO:0000269|PubMed:9811546"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P25910"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:9811546"
FT DISULFID 239..267
FT /evidence="ECO:0000269|PubMed:9811546"
FT CONFLICT 36..37
FT /note="AS -> QR (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="Q -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 56..58
FT /note="TED -> RQH (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="L -> H (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:7O0O"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:7O0O"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:7O0O"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:2AIO"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:7O0O"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:7O0O"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:7O0O"
FT HELIX 81..90
FT /evidence="ECO:0007829|PDB:7O0O"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:7O0O"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:7O0O"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:7O0O"
FT HELIX 114..120
FT /evidence="ECO:0007829|PDB:7O0O"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:7O0O"
FT HELIX 129..136
FT /evidence="ECO:0007829|PDB:7O0O"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:7O0O"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:7O0O"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:7AFZ"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:7O0O"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:7O0O"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:7O0O"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:7O0O"
FT STRAND 186..194
FT /evidence="ECO:0007829|PDB:7O0O"
FT STRAND 197..203
FT /evidence="ECO:0007829|PDB:7O0O"
FT HELIX 223..235
FT /evidence="ECO:0007829|PDB:7O0O"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:7O0O"
FT HELIX 247..250
FT /evidence="ECO:0007829|PDB:7O0O"
FT HELIX 254..259
FT /evidence="ECO:0007829|PDB:7O0O"
FT TURN 260..263
FT /evidence="ECO:0007829|PDB:7O0O"
FT HELIX 267..287
FT /evidence="ECO:0007829|PDB:7O0O"
SQ SEQUENCE 290 AA; 30801 MW; 0B34CAB54518BC1E CRC64;
MRSTLLAFAL AVALPAAHTS AAEVPLPQLR AYTVDASWLQ PMAPLQIADH TWQIGTEDLT
ALLVQTPDGA VLLDGGMPQM ASHLLDNMKA RGVTPRDLRL ILLSHAHADH AGPVAELKRR
TGAKVAANAE SAVLLARGGS DDLHFGDGIT YPPANADRIV MDGEVITVGG IVFTAHFMAG
HTPGSTAWTW TDTRNGKPVR IAYADSLSAP GYQLQGNPRY PHLIEDYRRS FATVRALPCD
VLLTPHPGAS NWDYAAGARA GAKALTCKAY ADAAEQKFDG QLAKETAGAR
