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Protein

Metallo-beta-lactamase type 2

Gene

blaB1

Organism
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum)
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 chelating agents such as EDTA, 1-10 phenanthroline and pyridine-2,6-dicarboxylic acid.1 Publication

Kineticsi

Kcat is 350 sec(-1) for lactamase activity with imipenem as substrate. Kcat is 300 sec(-1) for lactamase activity with 6-beta-iodopenicillanate as substrate. Kcat is 280 sec(-1) for lactamase activity with penicillin G as substrate. Kcat is 39 sec(-1) for lactamase activity with cefotaxime as substrate. Kcat is 17 sec(-1) for lactamase activity with nitrocefin as substrate. Kcat is 14 sec(-1) for lactamase activity with cephaloridine as substrate. Kcat is 6 sec(-1) for lactamase activity with cefoxitin as substrate.1 Publication

Manual assertion based on experiment ini

  1. KM=24 µM for cefoxitin1 Publication
  2. KM=29 µM for cephaloridine1 Publication
  3. KM=32 µM for penicillin G1 Publication
  4. KM=43 µM for 6-beta-iodopenicillanate1 Publication
  5. KM=66 µM for nitrocefin1 Publication
  6. KM=180 µM for cefotaxime1 Publication
  7. KM=370 µM for imipenem1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi98Zinc 1; via tele nitrogen1 Publication1
    Metal bindingi100Zinc 1; via pros nitrogen1 Publication1
    Metal bindingi102Zinc 21 Publication1
    Metal bindingi161Zinc 1; via tele nitrogen1 Publication1
    Metal bindingi180Zinc 21 Publication1
    Binding sitei183Substrate1 Publication1
    Metal bindingi222Zinc 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

    BioCyciMetaCyc:MONOMER-13428.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Metallo-beta-lactamase type 2Curated (EC:3.5.2.61 Publication)
    Alternative name(s):
    B2 metallo-beta-lactamaseCurated
    Beta-lactamase type II1 Publication
    Carbapenem-hydrolyzing beta-lactamase BlaB-11 Publication
    Short name:
    CHbetaL-11 Publication
    Class B carbapenemase BlaB-11 Publication
    Metallo-beta-lactamase type II1 Publication
    Gene namesi
    Name:blaB1
    Synonyms:blaB1 Publication
    OrganismiElizabethkingia meningoseptica (Chryseobacterium meningosepticum)
    Taxonomic identifieri238 [NCBI]
    Taxonomic lineageiBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeElizabethkingia

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Periplasm

    Pathology & Biotechi

    Chemistry databases

    ChEMBLiCHEMBL1667692.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 221 PublicationAdd BLAST22
    ChainiPRO_000001694923 – 249Metallo-beta-lactamase type 2Add BLAST227

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Structurei

    Secondary structure

    1249
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi28 – 34Combined sources7
    Beta strandi37 – 46Combined sources10
    Beta strandi49 – 60Combined sources12
    Beta strandi63 – 68Combined sources6
    Helixi73 – 75Combined sources3
    Helixi76 – 87Combined sources12
    Beta strandi91 – 95Combined sources5
    Beta strandi97 – 100Combined sources4
    Turni101 – 103Combined sources3
    Helixi107 – 112Combined sources6
    Beta strandi116 – 120Combined sources5
    Helixi121 – 129Combined sources9
    Beta strandi136 – 141Combined sources6
    Beta strandi143 – 147Combined sources5
    Beta strandi150 – 155Combined sources6
    Beta strandi159 – 164Combined sources6
    Beta strandi167 – 170Combined sources4
    Turni171 – 174Combined sources4
    Beta strandi175 – 179Combined sources5
    Helixi198 – 211Combined sources14
    Turni212 – 214Combined sources3
    Beta strandi216 – 222Combined sources7

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1M2XX-ray1.50A/B/C/D27-222[»]
    ProteinModelPortaliO08498.
    SMRiO08498.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO08498.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    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.

    O08498-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MLKKIKISLI LALGLTSLQA FGQENPDVKI EKLKDNLYVY TTYNTFNGTK
    60 70 80 90 100
    YAANAVYLVT DKGVVVIDCP WGEDKFKSFT DEIYKKHGKK VIMNIATHSH
    110 120 130 140 150
    DDRAGGLEYF GKIGAKTYST KMTDSILAKE NKPRAQYTFD NNKSFKVGKS
    160 170 180 190 200
    EFQVYYPGKG HTADNVVVWF PKEKVLVGGC IIKSADSKDL GYIGEAYVND
    210 220 230 240
    WTQSVHNIQQ KFSGAQYVVA GHDDWKDQRS IQHTLDLINE YQQKQKASN
    Length:249
    Mass (Da):28,144
    Last modified:July 1, 1997 - v1
    Checksum:i0F042B5126E338F6
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X96858 Genomic DNA. Translation: CAA65601.1.
    AF189298 Genomic DNA. Translation: AAF89154.1.
    RefSeqiWP_029729112.1. NG_048691.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X96858 Genomic DNA. Translation: CAA65601.1.
    AF189298 Genomic DNA. Translation: AAF89154.1.
    RefSeqiWP_029729112.1. NG_048691.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1M2XX-ray1.50A/B/C/D27-222[»]
    ProteinModelPortaliO08498.
    SMRiO08498.
    ModBaseiSearch...
    MobiDBiSearch...

    Chemistry databases

    ChEMBLiCHEMBL1667692.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13428.

    Miscellaneous databases

    EvolutionaryTraceiO08498.

    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 nameiBLAB1_ELIME
    AccessioniPrimary (citable) accession number: O08498
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 23, 2003
    Last sequence update: July 1, 1997
    Last modified: November 2, 2016
    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

    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.