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O08498

- BLAB1_ELIME

UniProt

O08498 - BLAB1_ELIME

Protein

Carbapenem-hydrolyzing beta-lactamase BlaB-1

Gene

blaB1

Organism
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Hydrolyzes penicillins, cephalosporins (including cefoxitin), carbapenems and 6-beta-iodopenicillanate.

    Catalytic activityi

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

    Cofactori

    Binds 2 zinc ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi98 – 981Zinc 1By similarity
    Metal bindingi100 – 1001Zinc 1By similarity
    Metal bindingi102 – 1021Zinc 2By similarity
    Metal bindingi161 – 1611Zinc 1By similarity
    Metal bindingi180 – 1801Zinc 2By similarity
    Metal bindingi222 – 2221Zinc 2By similarity

    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

    BioCyciMetaCyc:MONOMER-13428.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbapenem-hydrolyzing beta-lactamase BlaB-1 (EC:3.5.2.6)
    Short name:
    CHbetaL-1
    Alternative name(s):
    Class B carbapenemase BlaB-1
    Gene namesi
    Name:blaB1
    Synonyms:blaB
    OrganismiElizabethkingia meningoseptica (Chryseobacterium meningosepticum)
    Taxonomic identifieri238 [NCBI]
    Taxonomic lineageiBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeElizabethkingia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 22221 PublicationAdd
    BLAST
    Chaini23 – 249227Carbapenem-hydrolyzing beta-lactamase BlaB-1PRO_0000016949Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1M2XX-ray1.50A/B/C/D27-245[»]
    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.
    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.
    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

    MLKKIKISLI LALGLTSLQA FGQENPDVKI EKLKDNLYVY TTYNTFNGTK    50
    YAANAVYLVT DKGVVVIDCP WGEDKFKSFT DEIYKKHGKK VIMNIATHSH 100
    DDRAGGLEYF GKIGAKTYST KMTDSILAKE NKPRAQYTFD NNKSFKVGKS 150
    EFQVYYPGKG HTADNVVVWF PKEKVLVGGC IIKSADSKDL GYIGEAYVND 200
    WTQSVHNIQQ KFSGAQYVVA GHDDWKDQRS IQHTLDLINE YQQKQKASN 249
    Length:249
    Mass (Da):28,144
    Last modified:July 1, 1997 - v1
    Checksum:i0F042B5126E338F6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X96858 Genomic DNA. Translation: CAA65601.1.
    AF189298 Genomic DNA. Translation: AAF89154.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X96858 Genomic DNA. Translation: CAA65601.1 .
    AF189298 Genomic DNA. Translation: AAF89154.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1M2X X-ray 1.50 A/B/C/D 27-245 [» ]
    ProteinModelPortali O08498.
    SMRi O08498. Positions 27-245.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    ChEMBLi CHEMBL1667692.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-13428.

    Miscellaneous databases

    EvolutionaryTracei O08498.

    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.
    PS00744. BETA_LACTAMASE_B_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization and sequence of the Chryseobacterium (Flavobacterium) meningosepticum carbapenemase: a new molecular class B beta-lactamase showing a broad substrate profile."
      Rossolini G.M., Franceschini N., Riccio M.L., Mercuri P.S., Perilli M., Galleni M., Frere J.-M., Amicosante G.
      Biochem. J. 332:145-152(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-27, CHARACTERIZATION.
      Strain: ATCC 13254 / CCUG 4310 / CIP 6058 / LMG 12280 / NCTC 10585.
    2. "Molecular and biochemical heterogeneity of class B carbapenem-hydrolyzing beta-lactamases in Chryseobacterium meningosepticum."
      Bellais S., Aubert D., Naas T., Nordmann P.
      Antimicrob. Agents Chemother. 44:1878-1886(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: PINT.

    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: October 1, 2014
    This is version 77 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