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Protein

Metallo-beta-lactamase type 2

Gene
N/A
Organism
Serratia marcescens
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring.1 Publication

Catalytic activityi

A beta-lactam + H2O = a substituted beta-amino acid.1 Publication

Cofactori

Zn2+1 PublicationNote: Binds 2 Zn2+ ions per subunit.1 Publication

Enzyme regulationi

Inhibited by captopril stereoisomers, Hg2+, Fe2+, Cu2+ and by chelating agents such as EDTA (PubMed:8141584, PubMed:26482303). This enzyme is not susceptible to inactivation by the beta-lactamase-blocking agents clavulanic acid or cloxacillin (PubMed:8141584).2 Publications

Kineticsi

  1. KM=0.74 µM for meropenem1 Publication
  2. KM=1.24 µM for ceftazidime1 Publication
  3. KM=2.07 µM for ceftizoxime and panipenem1 Publication
  4. KM=2.13 µM for cefoperazone1 Publication
  5. KM=2.15 µM for ampicillin1 Publication
  6. KM=3.97 µM for aztreonam1 Publication
  7. KM=7.33 µM for imipenem1 Publication
  8. KM=7.55 µM for moxalactam1 Publication
  9. KM=7.74 µM for cephaloridine1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi95 – 951Zinc 1; via tele nitrogen1 Publication
    Metal bindingi97 – 971Zinc 1; via pros nitrogen1 Publication
    Metal bindingi99 – 991Zinc 21 Publication
    Metal bindingi157 – 1571Zinc 1; via tele nitrogen1 Publication
    Metal bindingi176 – 1761Zinc 21 Publication
    Binding sitei179 – 1791Substrate1 Publication
    Binding sitei185 – 1851Substrate; via amide nitrogenBy similarity
    Metal bindingi215 – 2151Zinc 2; via tele nitrogen1 Publication

    GO - Molecular functioni

    • beta-lactamase activity Source: UniProtKB
    • zinc ion binding Source: UniProtKB

    GO - Biological processi

    • antibiotic catabolic process Source: UniProtKB
    • response to antibiotic Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Antibiotic resistance

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi3.5.2.6. 5690.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Metallo-beta-lactamase type 2Curated (EC:3.5.2.61 Publication)
    Alternative name(s):
    B2 metallo-beta-lactamaseCurated
    BLA-IMP1 Publication
    Short name:
    IMP-11 Publication
    Beta-lactamase type II1 Publication
    Metallo-beta-lactamase type II1 Publication
    OrganismiSerratia marcescens
    Taxonomic identifieri615 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia

    Subcellular locationi

    Keywords - Cellular componenti

    Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 18181 PublicationAdd
    BLAST
    Chaini19 – 246228Metallo-beta-lactamase type 2PRO_0000016946Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Chemistry

    BindingDBiP52699.

    Structurei

    Secondary structure

    1
    246
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi26 – 316Combined sources
    Beta strandi34 – 4310Combined sources
    Turni44 – 463Combined sources
    Beta strandi47 – 5812Combined sources
    Beta strandi61 – 666Combined sources
    Helixi71 – 8313Combined sources
    Beta strandi87 – 926Combined sources
    Beta strandi94 – 974Combined sources
    Helixi98 – 1014Combined sources
    Helixi104 – 1096Combined sources
    Beta strandi114 – 1174Combined sources
    Helixi118 – 1269Combined sources
    Beta strandi133 – 1364Combined sources
    Beta strandi138 – 1447Combined sources
    Turni145 – 1473Combined sources
    Beta strandi148 – 1514Combined sources
    Beta strandi155 – 1584Combined sources
    Beta strandi163 – 1664Combined sources
    Turni167 – 1704Combined sources
    Beta strandi171 – 1755Combined sources
    Turni191 – 1933Combined sources
    Helixi194 – 20512Combined sources
    Beta strandi209 – 2168Combined sources
    Helixi222 – 23817Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DD6X-ray2.00A/B19-246[»]
    1VGNX-ray2.63A/B19-246[»]
    1WUOX-ray2.01A/B/C/D19-246[»]
    1WUPX-ray3.00A/B/C/D19-246[»]
    2DOOX-ray2.43A/B19-246[»]
    4C1FX-ray2.01A/B19-246[»]
    4C1GX-ray1.71A/B19-246[»]
    ProteinModelPortaliP52699.
    SMRiP52699. Positions 19-239.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP52699.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    KOiK18782.

    Family and domain databases

    Gene3Di3.60.15.10. 1 hit.
    InterProiIPR001018. Beta-lactamase_class-B_CS.
    IPR001279. Metallo-B-lactamas.
    [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.
    PS00744. BETA_LACTAMASE_B_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P52699-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSKLSVFFIF LFCSIATAAE SLPDLKIEKL DEGVYVHTSF EEVNGWGVVP
    60 70 80 90 100
    KHGLVVLVNA EAYLIDTPFT AKDTEKLVTW FVERGYKIKG SISSHFHSDS
    110 120 130 140 150
    TGGIEWLNSR SIPTYASELT NELLKKDGKV QATNSFSGVN YWLVKNKIEV
    160 170 180 190 200
    FYPGPGHTPD NVVVWLPERK ILFGGCFIKP YGLGNLGDAN IEAWPKSAKL
    210 220 230 240
    LKSKYGKAKL VVPSHSEVGD ASLLKLTLEQ AVKGLNESKK PSKPSN
    Length:246
    Mass (Da):27,120
    Last modified:October 1, 1996 - v1
    Checksum:i9B2599E8F1B22D36
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    S71932 Genomic DNA. Translation: AAB30289.1.
    D50438 Genomic DNA. Translation: BAA08930.1.

    Genome annotation databases

    KEGGiag:AAB30289.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    S71932 Genomic DNA. Translation: AAB30289.1.
    D50438 Genomic DNA. Translation: BAA08930.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DD6X-ray2.00A/B19-246[»]
    1VGNX-ray2.63A/B19-246[»]
    1WUOX-ray2.01A/B/C/D19-246[»]
    1WUPX-ray3.00A/B/C/D19-246[»]
    2DOOX-ray2.43A/B19-246[»]
    4C1FX-ray2.01A/B19-246[»]
    4C1GX-ray1.71A/B19-246[»]
    ProteinModelPortaliP52699.
    SMRiP52699. Positions 19-239.
    ModBaseiSearch...
    MobiDBiSearch...

    Chemistry

    BindingDBiP52699.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:AAB30289.

    Phylogenomic databases

    KOiK18782.

    Enzyme and pathway databases

    BRENDAi3.5.2.6. 5690.

    Miscellaneous databases

    EvolutionaryTraceiP52699.

    Family and domain databases

    Gene3Di3.60.15.10. 1 hit.
    InterProiIPR001018. Beta-lactamase_class-B_CS.
    IPR001279. Metallo-B-lactamas.
    [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.
    PS00744. BETA_LACTAMASE_B_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "Molecular characterization of an enterobacterial metallo beta-lactamase found in a clinical isolate of Serratia marcescens that shows imipenem resistance."
      Osano E., Arakawa Y., Wacharotayankun R., Ohta M., Horii T., Ito H., Yoshimura F., Kato N.
      Antimicrob. Agents Chemother. 38:71-78(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 19-42, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBSTRATE SPECIFICITY.
      Strain: AK9373 / TN9106.
    2. Cited for: X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) OF 19-246 IN COMPLEX WITH SUBSTRATE ANALOG AND ZINC IONS, ENZYME REGULATION, COFACTOR.

    Entry informationi

    Entry nameiBLAB_SERMA
    AccessioniPrimary (citable) accession number: P52699
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: April 13, 2016
    This is version 86 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.