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P52700 (BLA1_STEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Metallo-beta-lactamase L1

EC=3.5.2.6
Alternative name(s):
Beta-lactamase type II
Penicillinase
OrganismStenotrophomonas maltophilia (Pseudomonas maltophilia) (Xanthomonas maltophilia)
Taxonomic identifier40324 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeStenotrophomonasStenotrophomonas maltophilia group

Protein attributes

Sequence length290 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 metallo-beta-lactamase superfamily. Class-B beta-lactamase family.

Biophysicochemical properties

pH dependence:

Unstable below pH 8, unless zinc is present.

Ontologies

Keywords
   Biological processAntibiotic resistance
   Cellular componentPeriplasm
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processantibiotic catabolic process

Inferred from electronic annotation. Source: InterPro

response to antibiotic

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbeta-lactamase activity

Inferred from electronic annotation. Source: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 3312
PRO_0000016947
Chain34 – 290257Metallo-beta-lactamase L1
PRO_0000016948

Sites

Metal binding1051Zinc 1
Metal binding1071Zinc 1
Metal binding1091Zinc 2
Metal binding1811Zinc 1
Metal binding2051Zinc 2
Metal binding2171Zinc 2

Amino acid modifications

Disulfide bond239 ↔ 267

Experimental info

Sequence conflict36 – 372AS → QR AA sequence Ref.2
Sequence conflict401Q → A AA sequence Ref.2
Sequence conflict56 – 583TED → RQH AA sequence Ref.2
Sequence conflict631L → H AA sequence Ref.2

Secondary structure

....................................................... 290
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P52700 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 0B34CAB54518BC1E

FASTA29030,801
        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 

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X75074 Genomic DNA. Translation: CAA52968.1.
PIRS45349.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SMLX-ray1.70A22-290[»]
2AIOX-ray1.70A22-290[»]
2FM6X-ray1.75A/B22-290[»]
2FU6X-ray2.05A/B22-290[»]
2FU7X-ray1.85A/B22-290[»]
2FU8X-ray1.80A/B22-290[»]
2FU9X-ray1.80A/B22-290[»]
2GFJX-ray1.80A/B22-290[»]
2GFKX-ray1.90A/B22-290[»]
2H6AX-ray1.80A/B22-290[»]
2HB9X-ray1.75A22-290[»]
2QDTX-ray2.00A22-290[»]
2QINX-ray1.76A/B/C/D22-290[»]
2QJSX-ray2.25A/B/C/D22-290[»]
ProteinModelPortalP52700.
SMRP52700. Positions 23-288.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP52700.
ChEMBLCHEMBL3326.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP52700.

Family and domain databases

Gene3D3.60.15.10. 1 hit.
InterProIPR001279. Beta-lactamas-like.
IPR001018. Beta-lactamase_class-B_CS.
[Graphical view]
PfamPF00753. Lactamase_B. 1 hit.
[Graphical view]
SMARTSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMSSF56281. SSF56281. 1 hit.
PROSITEPS00743. BETA_LACTAMASE_B_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP52700.

Entry information

Entry nameBLA1_STEMA
AccessionPrimary (citable) accession number: P52700
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references