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P52700

- BLA1_STEMA

UniProt

P52700 - BLA1_STEMA

Protein

Metallo-beta-lactamase L1

Gene
N/A
Organism
Stenotrophomonas maltophilia (Pseudomonas maltophilia) (Xanthomonas maltophilia)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Has a high activity against imipenem.

    Catalytic activityi

    A beta-lactam + H2O = a substituted beta-amino acid.

    Cofactori

    Binds 2 zinc ions per subunit.

    Enzyme regulationi

    Inhibited by Hg2+ or Cu2+. Reduced enzymatic activity in presence of Cobalt, Nickel, Cadmium, and Manganese.

    pH dependencei

    Unstable below pH 8, unless zinc is present.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi105 – 1051Zinc 1
    Metal bindingi107 – 1071Zinc 1
    Metal bindingi109 – 1091Zinc 2
    Metal bindingi181 – 1811Zinc 1
    Metal bindingi205 – 2051Zinc 2
    Metal bindingi217 – 2171Zinc 2

    GO - Molecular functioni

    1. beta-lactamase activity Source: UniProtKB-EC
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. antibiotic catabolic process Source: InterPro
    2. response to antibiotic Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Antibiotic resistance

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    SABIO-RKP52700.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Metallo-beta-lactamase L1 (EC:3.5.2.6)
    Alternative name(s):
    Beta-lactamase type II
    Penicillinase
    OrganismiStenotrophomonas maltophilia (Pseudomonas maltophilia) (Xanthomonas maltophilia)
    Taxonomic identifieri40324 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeStenotrophomonasStenotrophomonas maltophilia group

    Subcellular locationi

    Periplasm Curated

    GO - Cellular componenti

    1. periplasmic space Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Propeptidei22 – 33121 PublicationPRO_0000016947Add
    BLAST
    Chaini34 – 290257Metallo-beta-lactamase L1PRO_0000016948Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi239 ↔ 267

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Homotetramer.

    Structurei

    Secondary structure

    1
    290
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi36 – 394
    Beta strandi45 – 484
    Beta strandi51 – 533
    Beta strandi55 – 595
    Beta strandi62 – 665
    Beta strandi69 – 735
    Helixi78 – 803
    Helixi81 – 9010
    Helixi95 – 973
    Beta strandi98 – 1025
    Helixi108 – 1114
    Helixi114 – 1207
    Beta strandi124 – 1274
    Helixi129 – 1368
    Turni137 – 1393
    Turni143 – 1453
    Turni147 – 1493
    Beta strandi157 – 1593
    Beta strandi165 – 1684
    Beta strandi171 – 1777
    Beta strandi180 – 1823
    Beta strandi186 – 1949
    Beta strandi197 – 2037
    Helixi223 – 23513
    Beta strandi240 – 2434
    Helixi247 – 2504
    Helixi254 – 2596
    Turni260 – 2634
    Helixi267 – 28721

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP52700.
    SMRiP52700. Positions 23-288.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP52700.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.60.15.10. 1 hit.
    InterProiIPR001279. Beta-lactamas-like.
    IPR001018. Beta-lactamase_class-B_CS.
    [Graphical view]
    PfamiPF00753. Lactamase_B. 1 hit.
    [Graphical view]
    SMARTiSM00849. Lactamase_B. 1 hit.
    [Graphical view]
    SUPFAMiSSF56281. SSF56281. 1 hit.
    PROSITEiPS00743. BETA_LACTAMASE_B_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P52700-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRSTLLAFAL AVALPAAHTS AAEVPLPQLR AYTVDASWLQ PMAPLQIADH    50
    TWQIGTEDLT ALLVQTPDGA VLLDGGMPQM ASHLLDNMKA RGVTPRDLRL 100
    ILLSHAHADH AGPVAELKRR TGAKVAANAE SAVLLARGGS DDLHFGDGIT 150
    YPPANADRIV MDGEVITVGG IVFTAHFMAG HTPGSTAWTW TDTRNGKPVR 200
    IAYADSLSAP GYQLQGNPRY PHLIEDYRRS FATVRALPCD VLLTPHPGAS 250
    NWDYAAGARA GAKALTCKAY ADAAEQKFDG QLAKETAGAR 290
    Length:290
    Mass (Da):30,801
    Last modified:October 1, 1996 - v1
    Checksum:i0B34CAB54518BC1E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti36 – 372AS → QR AA sequence (PubMed:3931629)Curated
    Sequence conflicti40 – 401Q → A AA sequence (PubMed:3931629)Curated
    Sequence conflicti56 – 583TED → RQH AA sequence (PubMed:3931629)Curated
    Sequence conflicti63 – 631L → H AA sequence (PubMed:3931629)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75074 Genomic DNA. Translation: CAA52968.1.
    PIRiS45349.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75074 Genomic DNA. Translation: CAA52968.1 .
    PIRi S45349.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali P52700.
    SMRi P52700. Positions 23-288.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P52700.
    ChEMBLi CHEMBL3326.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P52700.

    Miscellaneous databases

    EvolutionaryTracei P52700.

    Family and domain databases

    Gene3Di 3.60.15.10. 1 hit.
    InterProi IPR001279. Beta-lactamas-like.
    IPR001018. Beta-lactamase_class-B_CS.
    [Graphical view ]
    Pfami PF00753. Lactamase_B. 1 hit.
    [Graphical view ]
    SMARTi SM00849. Lactamase_B. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56281. SSF56281. 1 hit.
    PROSITEi PS00743. BETA_LACTAMASE_B_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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).

    Entry informationi

    Entry nameiBLA1_STEMA
    AccessioniPrimary (citable) accession number: P52700
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 88 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3