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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)DescriptionActionsGraphical viewLength
    Metal bindingi95Zinc 1; via tele nitrogen1 Publication1
    Metal bindingi97Zinc 1; via pros nitrogen1 Publication1
    Metal bindingi99Zinc 21 Publication1
    Metal bindingi157Zinc 1; via tele nitrogen1 Publication1
    Metal bindingi176Zinc 21 Publication1
    Binding sitei179Substrate1 Publication1
    Binding sitei185Substrate; via amide nitrogenBy similarity1
    Metal bindingi215Zinc 2; via tele nitrogen1 Publication1

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesYersiniaceaeSerratia

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 181 PublicationAdd BLAST18
    ChainiPRO_000001694619 – 246Metallo-beta-lactamase type 2Add BLAST228

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    Secondary structure

    1246
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi26 – 31Combined sources6
    Beta strandi34 – 43Combined sources10
    Turni44 – 46Combined sources3
    Beta strandi47 – 58Combined sources12
    Beta strandi61 – 66Combined sources6
    Helixi71 – 83Combined sources13
    Beta strandi87 – 92Combined sources6
    Beta strandi94 – 97Combined sources4
    Helixi98 – 101Combined sources4
    Helixi104 – 109Combined sources6
    Beta strandi114 – 117Combined sources4
    Helixi118 – 126Combined sources9
    Beta strandi133 – 136Combined sources4
    Beta strandi138 – 144Combined sources7
    Turni145 – 147Combined sources3
    Beta strandi148 – 151Combined sources4
    Beta strandi155 – 158Combined sources4
    Beta strandi163 – 166Combined sources4
    Turni167 – 170Combined sources4
    Beta strandi171 – 175Combined sources5
    Turni191 – 193Combined sources3
    Helixi194 – 205Combined sources12
    Beta strandi209 – 216Combined sources8
    Helixi222 – 238Combined sources17

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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[»]
    5EV6X-ray1.98A/B/C/D19-246[»]
    5EV8X-ray2.30A/B/C/D19-246[»]
    5EWAX-ray2.30A/B/C/D19-246[»]
    ProteinModelPortaliP52699.
    SMRiP52699.
    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.
    RefSeqiWP_003159548.1. NG_049172.1.

    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.
    RefSeqiWP_003159548.1. NG_049172.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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[»]
    5EV6X-ray1.98A/B/C/D19-246[»]
    5EV8X-ray2.30A/B/C/D19-246[»]
    5EWAX-ray2.30A/B/C/D19-246[»]
    ProteinModelPortaliP52699.
    SMRiP52699.
    ModBaseiSearch...
    MobiDBiSearch...

    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...

    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: November 2, 2016
    This is version 91 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.