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P04190

- BLA2_BACCE

UniProt

P04190 - BLA2_BACCE

Protein

Beta-lactamase 2

Gene

blm

Organism
Bacillus cereus
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (20 Mar 1987)
      Previous versions | rss
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    Functioni

    Can hydrolyze carbapenem compounds.

    Catalytic activityi

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

    Cofactori

    Binds 2 zinc ions per subunit. The enzyme can also function with only 1 zinc ion.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi116 – 1161Zinc 1; high-affinity
    Metal bindingi118 – 1181Zinc 1; high-affinity
    Metal bindingi120 – 1201Zinc 2; low-affinity
    Metal bindingi179 – 1791Zinc 1; high-affinity
    Metal bindingi198 – 1981Zinc 2; low-affinity
    Metal bindingi240 – 2401Zinc 2; low-affinity

    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

    SABIO-RKP04190.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-lactamase 2 (EC:3.5.2.6)
    Alternative name(s):
    Beta-lactamase II
    Cephalosporinase
    Penicillinase
    Gene namesi
    Name:blm
    OrganismiBacillus cereus
    Taxonomic identifieri1396 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 30301 PublicationAdd
    BLAST
    Chaini31 – 257227Beta-lactamase 2PRO_0000016942Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    Secondary structure

    1
    257
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi38 – 403
    Beta strandi42 – 5211
    Beta strandi55 – 6410
    Beta strandi67 – 7812
    Beta strandi81 – 866
    Helixi91 – 10515
    Beta strandi109 – 1135
    Beta strandi116 – 1183
    Helixi119 – 1224
    Helixi125 – 1317
    Beta strandi134 – 1363
    Helixi139 – 1479
    Beta strandi159 – 1657
    Beta strandi168 – 1736
    Beta strandi178 – 1825
    Beta strandi185 – 1873
    Turni189 – 1913
    Beta strandi193 – 1975
    Beta strandi212 – 2143
    Helixi216 – 22914
    Beta strandi234 – 2418
    Helixi247 – 2559

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BC2X-ray1.90A/B31-257[»]
    1BMCX-ray2.50A37-257[»]
    1BVTX-ray1.85A31-257[»]
    1DXKX-ray1.85A31-257[»]
    1MQOX-ray1.35A31-257[»]
    2BC2X-ray1.70A/B31-257[»]
    2BFKX-ray2.00A/B31-257[»]
    2BFLX-ray1.80A/B31-257[»]
    2BFZX-ray2.30A/B31-191[»]
    2BG2X-ray2.40A/B31-257[»]
    2BG6X-ray2.30A/B31-257[»]
    2BG7X-ray2.10A/B31-257[»]
    2BG8X-ray2.50A/B31-257[»]
    2BGAX-ray2.70A/B31-257[»]
    2M5CNMR-A31-257[»]
    2M5DNMR-A31-257[»]
    2NXAX-ray2.29A37-257[»]
    2NYPX-ray1.84A37-257[»]
    2NZEX-ray1.80A/B36-257[»]
    2NZFX-ray2.28A37-257[»]
    2UYXX-ray1.95A30-257[»]
    3BC2X-ray1.70A31-257[»]
    3FCZX-ray2.80A/B36-247[»]
    3I0VX-ray1.60A31-257[»]
    3I11X-ray1.45A31-257[»]
    3I13X-ray1.74A31-257[»]
    3I14X-ray1.55A31-257[»]
    3I15X-ray1.55A31-257[»]
    3KNRX-ray1.71A/B/C/D31-257[»]
    3KNSX-ray1.58A/B/C/D31-257[»]
    ProteinModelPortaliP04190.
    SMRiP04190. Positions 37-247.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04190.

    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.

    P04190-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKNTLLKVG LCVGLLGTIQ FVSTISSVQA SQKVEKTVIK NETGTISISQ    50
    LNKNVWVHTE LGSFNGEAVP SNGLVLNTSK GLVLVDSSWD DKLTKELIEM 100
    VEKKFQKRVT DVIITHAHAD RIGGIKTLKE RGIKAHSTAL TAELAKKNGY 150
    EEPLGDLQTV TNLKFGNMKV ETFYPGKGHT EDNIVVWLPQ YNILVGGCLV 200
    KSTSAKDLGN VADAYVNEWS TSIENVLKRY RNINAVVPGH GEVGDKGLLL 250
    HTLDLLK 257
    Length:257
    Mass (Da):28,092
    Last modified:March 20, 1987 - v1
    Checksum:i268EBFB7DDA45431
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11189 Genomic DNA. Translation: AAA22276.1.
    PIRiA91806. PNBSU2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11189 Genomic DNA. Translation: AAA22276.1 .
    PIRi A91806. PNBSU2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BC2 X-ray 1.90 A/B 31-257 [» ]
    1BMC X-ray 2.50 A 37-257 [» ]
    1BVT X-ray 1.85 A 31-257 [» ]
    1DXK X-ray 1.85 A 31-257 [» ]
    1MQO X-ray 1.35 A 31-257 [» ]
    2BC2 X-ray 1.70 A/B 31-257 [» ]
    2BFK X-ray 2.00 A/B 31-257 [» ]
    2BFL X-ray 1.80 A/B 31-257 [» ]
    2BFZ X-ray 2.30 A/B 31-191 [» ]
    2BG2 X-ray 2.40 A/B 31-257 [» ]
    2BG6 X-ray 2.30 A/B 31-257 [» ]
    2BG7 X-ray 2.10 A/B 31-257 [» ]
    2BG8 X-ray 2.50 A/B 31-257 [» ]
    2BGA X-ray 2.70 A/B 31-257 [» ]
    2M5C NMR - A 31-257 [» ]
    2M5D NMR - A 31-257 [» ]
    2NXA X-ray 2.29 A 37-257 [» ]
    2NYP X-ray 1.84 A 37-257 [» ]
    2NZE X-ray 1.80 A/B 36-257 [» ]
    2NZF X-ray 2.28 A 37-257 [» ]
    2UYX X-ray 1.95 A 30-257 [» ]
    3BC2 X-ray 1.70 A 31-257 [» ]
    3FCZ X-ray 2.80 A/B 36-247 [» ]
    3I0V X-ray 1.60 A 31-257 [» ]
    3I11 X-ray 1.45 A 31-257 [» ]
    3I13 X-ray 1.74 A 31-257 [» ]
    3I14 X-ray 1.55 A 31-257 [» ]
    3I15 X-ray 1.55 A 31-257 [» ]
    3KNR X-ray 1.71 A/B/C/D 31-257 [» ]
    3KNS X-ray 1.58 A/B/C/D 31-257 [» ]
    ProteinModelPortali P04190.
    SMRi P04190. Positions 37-247.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P04190.

    Miscellaneous databases

    EvolutionaryTracei P04190.

    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. "Cloning and sequencing of the metallothioprotein beta-lactamase II gene of Bacillus cereus 569/H in Escherichia coli."
      Hussain M., Carlino A., Madonna M.J., Lampen J.O.
      J. Bacteriol. 164:223-229(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 569/H / NCTC 9945.
    2. "The amino acid sequence of the zinc-requiring beta-lactamase II from the bacterium Bacillus cereus 569."
      Ambler R.P., Daniel M., Fleming J., Hermoso J.M., Pang C., Waley S.G.
      FEBS Lett. 189:207-211(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 31-183; 187-210 AND 214-257.
      Strain: 569/H / NCTC 9945.
    3. "An X-ray-crystallographic study of beta-lactamase II from Bacillus cereus at 0.35-nm resolution."
      Sutton B.J., Artymiuk P.J., Cordero-Borboa A.E., Little C., Phillips D.C., Waley S.G.
      Biochem. J. 248:181-188(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
    4. "The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold."
      Carfi A., Pares S., Duee E., Galleni M., Duez C., Frere J.-M., Dideberg O.
      EMBO J. 14:4914-4921(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    5. "1.85-A resolution structure of the zinc (II) beta-lactamase from Bacillus cereus."
      Carfi A., Duee E., Galleni M., Frere J.-M., Dideberg O.
      Acta Crystallogr. D 54:313-323(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
    6. "Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9-A resolution: binuclear active site with features of a mononuclear enzyme."
      Fabiane S.M., Sohi M.K., Wan T., Payne D.J., Bateson J.H., Mitchell T., Sutton B.J.
      Biochemistry 37:12404-12411(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
      Strain: 569/H / NCTC 9945.
    7. "Structural effects of the active site mutation cysteine to serine in Bacillus cereus zinc-beta-lactamase."
      Chantalat L., Duee E., Galleni M., Frere J.-M., Dideberg O.
      Protein Sci. 9:1402-1406(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT SER-198.
      Strain: 569/H / NCTC 9945.

    Entry informationi

    Entry nameiBLA2_BACCE
    AccessioniPrimary (citable) accession number: P04190
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 1987
    Last sequence update: March 20, 1987
    Last modified: October 1, 2014
    This is version 100 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