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Metallo-beta-lactamase L1 type 3 (EC 3.5.2.6) (B3 metallo-beta-lactamase) (Beta-lactamase type III) (Metallo-beta-lactamase L1 type III) (Penicillinase)

 BLA1_STEMA              Reviewed;         290 AA.
P52700;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 101.
RecName: Full=Metallo-beta-lactamase L1 type 3 {ECO:0000305};
EC=3.5.2.6 {ECO:0000269|PubMed:3931629};
AltName: Full=B3 metallo-beta-lactamase {ECO:0000305};
AltName: Full=Beta-lactamase type III {ECO:0000303|PubMed:3931629};
AltName: Full=Metallo-beta-lactamase L1 type III {ECO:0000303|PubMed:3931629};
AltName: Full=Penicillinase {ECO:0000303|PubMed:3931629};
Flags: Precursor;
Stenotrophomonas maltophilia (Pseudomonas maltophilia) (Xanthomonas
maltophilia).
Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
Xanthomonadaceae; Stenotrophomonas;
Stenotrophomonas maltophilia group.
NCBI_TaxID=40324;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=IID 1275;
PubMed=8018721; DOI=10.1016/0167-4781(94)90011-6;
Walsh T.R., Hall L., Assinder S.J., Nichols W.W., Cartwright S.J.,
Macgowan A.P., Bennett P.M.;
"Sequence analysis of the L1 metallo-beta-lactamase from Xanthomonas
maltophilia.";
Biochim. Biophys. Acta 1218:199-201(1994).
[2]
PROTEIN SEQUENCE OF 34-65, FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND SUBUNIT.
STRAIN=IID 1275;
PubMed=3931629; DOI=10.1042/bj2290791;
Bicknell R., Emanuel E.L., Gagnon J., Waley S.G.;
"The production and molecular properties of the zinc beta-lactamase of
Pseudomonas maltophilia IID 1275.";
Biochem. J. 229:791-797(1985).
[3]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 22-290 IN COMPLEX WITH ZINC
IONS, FUNCTION, COFACTOR, SUBUNIT, DISULFIDE BOND, AND REACTION
MECHANISM.
PubMed=9811546; DOI=10.1006/jmbi.1998.2148;
Ullah J.H., Walsh T.R., Taylor I.A., Emery D.C., Verma C.S.,
Gamblin S.J., Spencer J.;
"The crystal structure of the L1 metallo-beta-lactamase from
Stenotrophomonas maltophilia at 1.7 A resolution.";
J. Mol. Biol. 284:125-136(1998).
[4]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 22-290 IN COMPLEX WITH
SUBSTRATE ANALOGS AND ZINC, COFACTOR, AND SUBUNIT.
PubMed=17999929; DOI=10.1016/j.jmb.2007.10.036;
Nauton L., Kahn R., Garau G., Hernandez J.F., Dideberg O.;
"Structural insights into the design of inhibitors for the L1 metallo-
beta-lactamase from Stenotrophomonas maltophilia.";
J. Mol. Biol. 375:257-269(2008).
-!- FUNCTION: Confers resistance to the different beta-lactams
antibiotics (penicillin, cephalosporin and carbapenem) via the
hydrolysis of the beta-lactam ring. {ECO:0000269|PubMed:3931629,
ECO:0000269|PubMed:9811546}.
-!- CATALYTIC ACTIVITY: A beta-lactam + H(2)O = a substituted beta-
amino acid. {ECO:0000269|PubMed:3931629}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:17999929,
ECO:0000269|PubMed:9811546};
Note=Binds 2 Zn(2+) ions per subunit.
{ECO:0000269|PubMed:17999929, ECO:0000269|PubMed:9811546};
-!- ENZYME REGULATION: Inhibited by Hg(2+) or Cu(2+), and by chelating
agents such as EDTA and O-phenanthroline. Reduced enzymatic
activity in presence of cobalt, nickel, cadmium, and manganese.
{ECO:0000269|PubMed:3931629}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Unstable below pH 8, unless zinc is present.
{ECO:0000269|PubMed:3931629};
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17999929,
ECO:0000269|PubMed:3931629, ECO:0000269|PubMed:9811546}.
-!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
-!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
Class-B beta-lactamase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X75074; CAA52968.1; -; Genomic_DNA.
PIR; S45349; S45349.
PDB; 1SML; X-ray; 1.70 A; A=22-290.
PDB; 2AIO; X-ray; 1.70 A; A=22-290.
PDB; 2FM6; X-ray; 1.75 A; A/B=22-290.
PDB; 2FU6; X-ray; 2.05 A; A/B=22-290.
PDB; 2FU7; X-ray; 1.85 A; A/B=22-290.
PDB; 2FU8; X-ray; 1.80 A; A/B=22-290.
PDB; 2FU9; X-ray; 1.80 A; A/B=22-290.
PDB; 2GFJ; X-ray; 1.80 A; A/B=22-290.
PDB; 2GFK; X-ray; 1.90 A; A/B=22-290.
PDB; 2H6A; X-ray; 1.80 A; A/B=22-290.
PDB; 2HB9; X-ray; 1.75 A; A=22-290.
PDB; 2QDT; X-ray; 2.00 A; A=22-290.
PDB; 2QIN; X-ray; 1.76 A; A/B/C/D=22-290.
PDB; 2QJS; X-ray; 2.25 A; A/B/C/D=22-290.
PDB; 5DPX; X-ray; 1.85 A; A/B=22-290.
PDB; 5EVB; X-ray; 1.84 A; A=22-290.
PDB; 5EVD; X-ray; 1.80 A; A=22-290.
PDB; 5EVK; X-ray; 1.63 A; A=22-290.
PDB; 5HH5; X-ray; 1.80 A; A=22-290.
PDB; 5HH6; X-ray; 1.80 A; A=22-290.
PDBsum; 1SML; -.
PDBsum; 2AIO; -.
PDBsum; 2FM6; -.
PDBsum; 2FU6; -.
PDBsum; 2FU7; -.
PDBsum; 2FU8; -.
PDBsum; 2FU9; -.
PDBsum; 2GFJ; -.
PDBsum; 2GFK; -.
PDBsum; 2H6A; -.
PDBsum; 2HB9; -.
PDBsum; 2QDT; -.
PDBsum; 2QIN; -.
PDBsum; 2QJS; -.
PDBsum; 5DPX; -.
PDBsum; 5EVB; -.
PDBsum; 5EVD; -.
PDBsum; 5EVK; -.
PDBsum; 5HH5; -.
PDBsum; 5HH6; -.
ProteinModelPortal; P52700; -.
SMR; P52700; -.
BindingDB; P52700; -.
ChEMBL; CHEMBL3326; -.
DrugBank; DB02032; 1-(3-Mercapto-2-Methyl-Propionyl)-Pyrrolidine-2-Carboxylic Acid.
DrugBank; DB04740; MOXALACTAM (HYDROLYZED).
DrugBank; DB07939; N-(3-MERCAPTOPROPANOYL)-D-ALANINE.
DrugBank; DB08199; N-[(BENZYLOXY)CARBONYL]-L-CYSTEINYLGLYCINE.
BRENDA; 3.5.2.6; 5134.
SABIO-RK; P52700; -.
EvolutionaryTrace; P52700; -.
GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
GO; GO:0008800; F:beta-lactamase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0017001; P:antibiotic catabolic process; IDA:UniProtKB.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
Gene3D; 3.60.15.10; -; 1.
InterPro; IPR001018; Beta-lactamase_class-B_CS.
InterPro; IPR001279; Metallo-B-lactamas.
InterPro; IPR036866; Metallo-hydrolase/OxRdtase.
Pfam; PF00753; Lactamase_B; 1.
SMART; SM00849; Lactamase_B; 1.
SUPFAM; SSF56281; SSF56281; 1.
PROSITE; PS00743; BETA_LACTAMASE_B_1; 1.
1: Evidence at protein level;
3D-structure; Antibiotic resistance; Direct protein sequencing;
Disulfide bond; Hydrolase; Metal-binding; Periplasm; Signal; Zinc.
SIGNAL 1 21 {ECO:0000255}.
PROPEP 22 33 {ECO:0000269|PubMed:3931629}.
/FTId=PRO_0000016947.
CHAIN 34 290 Metallo-beta-lactamase L1 type 3.
/FTId=PRO_0000016948.
METAL 105 105 Zinc 1; via tele nitrogen.
{ECO:0000269|PubMed:17999929,
ECO:0000269|PubMed:9811546}.
METAL 107 107 Zinc 1; via pros nitrogen.
{ECO:0000269|PubMed:17999929,
ECO:0000269|PubMed:9811546}.
METAL 109 109 Zinc 2. {ECO:0000269|PubMed:17999929,
ECO:0000269|PubMed:9811546}.
METAL 110 110 Zinc 2; via tele nitrogen.
{ECO:0000269|PubMed:17999929,
ECO:0000269|PubMed:9811546}.
METAL 181 181 Zinc 1; via tele nitrogen.
{ECO:0000269|PubMed:17999929,
ECO:0000269|PubMed:9811546}.
METAL 246 246 Zinc 2; via tele nitrogen.
{ECO:0000269|PubMed:9811546}.
BINDING 205 205 Substrate.
{ECO:0000250|UniProtKB:P25910}.
DISULFID 239 267 {ECO:0000269|PubMed:9811546}.
CONFLICT 36 37 AS -> QR (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 40 40 Q -> A (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 56 58 TED -> RQH (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 63 63 L -> H (in Ref. 2; AA sequence).
{ECO:0000305}.
HELIX 36 39 {ECO:0000244|PDB:5EVK}.
STRAND 45 48 {ECO:0000244|PDB:5EVK}.
STRAND 51 53 {ECO:0000244|PDB:5EVK}.
STRAND 55 59 {ECO:0000244|PDB:2AIO}.
STRAND 62 66 {ECO:0000244|PDB:5EVK}.
STRAND 69 73 {ECO:0000244|PDB:5EVK}.
HELIX 78 80 {ECO:0000244|PDB:5EVK}.
HELIX 81 90 {ECO:0000244|PDB:5EVK}.
HELIX 95 97 {ECO:0000244|PDB:5EVK}.
STRAND 98 102 {ECO:0000244|PDB:5EVK}.
TURN 108 110 {ECO:0000244|PDB:5EVK}.
HELIX 114 120 {ECO:0000244|PDB:5EVK}.
STRAND 124 127 {ECO:0000244|PDB:5EVK}.
HELIX 129 136 {ECO:0000244|PDB:5EVK}.
TURN 137 139 {ECO:0000244|PDB:5EVK}.
TURN 143 145 {ECO:0000244|PDB:5EVK}.
TURN 147 149 {ECO:0000244|PDB:2AIO}.
STRAND 157 159 {ECO:0000244|PDB:5EVK}.
STRAND 165 168 {ECO:0000244|PDB:5EVK}.
STRAND 171 177 {ECO:0000244|PDB:5EVK}.
STRAND 180 182 {ECO:0000244|PDB:5EVK}.
STRAND 186 194 {ECO:0000244|PDB:5EVK}.
STRAND 197 203 {ECO:0000244|PDB:5EVK}.
HELIX 223 235 {ECO:0000244|PDB:5EVK}.
STRAND 240 243 {ECO:0000244|PDB:5EVK}.
HELIX 247 250 {ECO:0000244|PDB:5EVK}.
HELIX 254 259 {ECO:0000244|PDB:5EVK}.
TURN 260 263 {ECO:0000244|PDB:5EVK}.
HELIX 267 287 {ECO:0000244|PDB:5EVK}.
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


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