Reviewed, UniProtKB/Swiss-Prot P52700 (BLA1_STEMA)

Names and origin

Protein names	Recommended name:     Metallo-beta-lactamase L1     EC=3.5.2.6 Alternative name(s):     Beta-lactamase type II     Penicillinase
Organism	Stenotrophomonas maltophilia (Pseudomonas maltophilia) (Xanthomonas maltophilia)
Taxonomic identifier	40324 [NCBI]
Taxonomic lineage	Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Stenotrophomonas

Protein attributes

Sequence length	290 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Has a high activity against imipenem.
Catalytic activity	A beta-lactam + H2O = a substituted beta-amino acid.
Cofactor	Binds 2 zinc ions per subunit.
Enzyme regulation	Inhibited by Hg2+ or Cu2+. Reduced enzymatic activity in presence of Cobalt, Nickel, Cadmium, and Manganese.
Subunit structure	Homotetramer.
Subcellular location	Periplasm Potential.
Sequence similarities	Belongs to the class-B beta-lactamase family.
Biophysicochemical properties	pH dependence: Unstable below pH 8, unless zinc is present.

Ontologies

Keywords
Biological process	Antibiotic resistance
Cellular component	Periplasm
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	antibiotic catabolic process Inferred from electronic annotation. Source: InterPro response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	beta-lactamase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Potential

Propeptide

22 – 33

12

PRO_0000016947

Chain

34 – 290

257

Metallo-beta-lactamase L1

PRO_0000016948

Sites

Metal binding

105

1

Zinc 1

Metal binding

107

1

Zinc 1

Metal binding

109

1

Zinc 2

Metal binding

181

1

Zinc 1

Metal binding

205

1

Zinc 2

Metal binding

217

1

Zinc 2

Amino acid modifications

Disulfide bond

239 ↔ 267

Experimental info

Sequence conflict

36 – 37

2

AS → QR AA sequence Ref.2

Sequence conflict

40

1

Q → A AA sequence Ref.2

Sequence conflict

56 – 58

3

TED → RQH AA sequence Ref.2

Sequence conflict

63

1

L → H AA sequence Ref.2

Secondary structure

1

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290

Helix Strand Turn

Details...

Helix

36 – 39

4

Beta strand

45 – 48

4

Beta strand

51 – 53

3

Beta strand

62 – 66

5

Beta strand

69 – 73

5

Helix

78 – 80

3

Helix

81 – 90

10

Helix

95 – 97

3

Beta strand

98 – 102

5

Helix

108 – 111

4

Helix

114 – 120

7

Beta strand

124 – 127

4

Helix

129 – 136

8

Turn

137 – 139

3

Turn

143 – 145

3

Beta strand

157 – 159

3

Beta strand

165 – 168

4

Beta strand

171 – 177

7

Beta strand

180 – 182

3

Beta strand

186 – 194

9

Beta strand

197 – 203

7

Helix

223 – 235

13

Beta strand

240 – 243

4

Helix

247 – 250

4

Helix

254 – 259

6

Turn

260 – 263

4

Helix

267 – 287

21

Sequences

	Sequence		Length	Mass (Da)
	P52700-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 0B34CAB54518BC1E	FASTA	290	30,801
	10 20 30 40 50 60 MRSTLLAFAL AVALPAAHTS AAEVPLPQLR AYTVDASWLQ PMAPLQIADH TWQIGTEDLT 70 80 90 100 110 120 ALLVQTPDGA VLLDGGMPQM ASHLLDNMKA RGVTPRDLRL ILLSHAHADH AGPVAELKRR 130 140 150 160 170 180 TGAKVAANAE SAVLLARGGS DDLHFGDGIT YPPANADRIV MDGEVITVGG IVFTAHFMAG 190 200 210 220 230 240 HTPGSTAWTW TDTRNGKPVR IAYADSLSAP GYQLQGNPRY PHLIEDYRRS FATVRALPCD 250 260 270 280 290 VLLTPHPGAS NWDYAAGARA GAKALTCKAY ADAAEQKFDG QLAKETAGAR

References

[1]	"Sequence analysis of the L1 metallo-beta-lactamase from Xanthomonas maltophilia." Walsh T.R., Hall L., Assinder S.J., Nichols W.W., Cartwright S.J., Macgowan A.P., Bennett P.M. Biochim. Biophys. Acta 1218:199-201(1994) [PubMed: 8018721] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: IID 1275.
[2]	"The production and molecular properties of the zinc beta-lactamase of Pseudomonas maltophilia IID 1275." Bicknell R., Emanuel E.L., Gagnon J., Waley S.G. Biochem. J. 229:791-797(1985) [PubMed: 3931629] [Abstract] Cited for: PROTEIN SEQUENCE OF 34-65. Strain: IID 1275.
[3]	"The crystal structure of the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia at 1.7 A resolution." Ullah J.H., Walsh T.R., Taylor I.A., Emery D.C., Verma C.S., Gamblin S.J., Spencer J. J. Mol. Biol. 284:125-136(1998) [PubMed: 9811546] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X75074 Genomic DNA. Translation: CAA52968.1.

PIR

S45349.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SML	X-ray	1.70	A	22-290	[»]
2AIO	X-ray	1.70	A	22-290	[»]
2FM6	X-ray	1.75	A/B	22-290	[»]
2FU6	X-ray	2.05	A/B	22-290	[»]
2FU7	X-ray	1.85	A/B	22-290	[»]
2FU8	X-ray	1.80	A/B	22-290	[»]
2FU9	X-ray	1.80	A/B	22-290	[»]
2GFJ	X-ray	1.80	A/B	22-290	[»]
2GFK	X-ray	1.90	A/B	22-290	[»]
2H6A	X-ray	1.80	A/B	22-290	[»]
2HB9	X-ray	1.75	A	22-290	[»]
2QDT	X-ray	2.00	A	22-290	[»]
2QIN	X-ray	1.76	A/B/C/D	22-290	[»]
2QJS	X-ray	2.25	A/B/C/D	22-290	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

3.5.2.6. 39210.

Family and domain databases

InterPro

IPR001018. Beta-lactamase_class-B_CS.
IPR001279. Blactmase-like.
[Graphical view]

Pfam

PF00753. Lactamase_B. 1 hit.
[Graphical view]

PROSITE

PS00743. BETA_LACTAMASE_B_1. 1 hit.
PS00744. BETA_LACTAMASE_B_2. False negative.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

BLA1_STEMA

Accession

Primary (citable) accession number: P52700

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)