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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

  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)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi98 – 981Zinc 1; via tele nitrogen1 Publication
    Metal bindingi100 – 1001Zinc 1; via pros nitrogen1 Publication
    Metal bindingi102 – 1021Zinc 21 Publication
    Metal bindingi161 – 1611Zinc 1; via tele nitrogen1 Publication
    Metal bindingi180 – 1801Zinc 21 Publication
    Binding sitei183 – 1831Substrate1 Publication
    Metal bindingi222 – 2221Zinc 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

    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

    ChEMBLiCHEMBL1667692.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 22221 PublicationAdd
    BLAST
    Chaini23 – 249227Metallo-beta-lactamase type 2PRO_0000016949Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Structurei

    Secondary structure

    1
    249
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi28 – 347Combined sources
    Beta strandi37 – 4610Combined sources
    Beta strandi49 – 6012Combined sources
    Beta strandi63 – 686Combined sources
    Helixi73 – 753Combined sources
    Helixi76 – 8712Combined sources
    Beta strandi91 – 955Combined sources
    Beta strandi97 – 1004Combined sources
    Turni101 – 1033Combined sources
    Helixi107 – 1126Combined sources
    Beta strandi116 – 1205Combined sources
    Helixi121 – 1299Combined sources
    Beta strandi136 – 1416Combined sources
    Beta strandi143 – 1475Combined sources
    Beta strandi150 – 1556Combined sources
    Beta strandi159 – 1646Combined sources
    Beta strandi167 – 1704Combined sources
    Turni171 – 1744Combined sources
    Beta strandi175 – 1795Combined sources
    Helixi198 – 21114Combined sources
    Turni212 – 2143Combined sources
    Beta strandi216 – 2227Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1M2XX-ray1.50A/B/C/D27-222[»]
    ProteinModelPortaliO08498.
    SMRiO08498. Positions 27-245.
    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.

    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1M2XX-ray1.50A/B/C/D27-222[»]
    ProteinModelPortaliO08498.
    SMRiO08498. Positions 27-245.
    ModBaseiSearch...
    MobiDBiSearch...

    Chemistry

    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: September 7, 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.