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P25910

- BLAB_BACFG

UniProt

P25910 - BLAB_BACFG

Protein

Beta-lactamase type II

Gene

ccrA

Organism
Bacteroides fragilis
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 May 1992)
      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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi99 – 991Zinc 11 Publication
    Metal bindingi101 – 1011Zinc 11 Publication
    Metal bindingi103 – 1031Zinc 2
    Metal bindingi162 – 1621Zinc 11 Publication
    Metal bindingi181 – 1811Zinc 2
    Metal bindingi223 – 2231Zinc 2

    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-RKP25910.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-lactamase type II (EC:3.5.2.6)
    Alternative name(s):
    Cephalosporinase
    Imipenem-cefoxitin hydrolyzing enzyme
    Penicillinase
    Gene namesi
    Name:ccrA
    Synonyms:cfiA
    OrganismiBacteroides fragilis
    Taxonomic identifieri817 [NCBI]
    Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Add
    BLAST
    Chaini18 – 249232Beta-lactamase type IIPRO_0000016945Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    Secondary structure

    1
    249
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi22 – 243
    Beta strandi25 – 328
    Beta strandi34 – 4613
    Turni47 – 493
    Beta strandi50 – 6112
    Beta strandi64 – 696
    Helixi74 – 8815
    Beta strandi91 – 966
    Beta strandi98 – 1014
    Helixi102 – 1054
    Helixi108 – 1136
    Beta strandi117 – 1215
    Helixi122 – 13110
    Beta strandi137 – 14812
    Beta strandi151 – 1566
    Beta strandi161 – 1633
    Beta strandi168 – 1703
    Turni172 – 1743
    Beta strandi176 – 1805
    Turni199 – 2013
    Helixi202 – 21211
    Beta strandi217 – 2248
    Helixi230 – 24617

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A7TX-ray1.85A/B18-249[»]
    1A8TX-ray2.55A/B18-249[»]
    1HLKX-ray2.50A/B21-247[»]
    1KR3X-ray2.50A/B18-249[»]
    1ZNBX-ray1.85A/B18-249[»]
    2BMIX-ray2.00A/B18-249[»]
    2ZNBX-ray2.15A/B18-249[»]
    3ZNBX-ray2.70A/B18-249[»]
    4ZNBX-ray2.65A/B18-249[»]
    ProteinModelPortaliP25910.
    SMRiP25910. Positions 20-249.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP25910.

    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.

    P25910-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKTVFILISM LFPVAVMAQK SVKISDDISI TQLSDKVYTY VSLAEIEGWG    50
    MVPSNGMIVI NNHQAALLDT PINDAQTEML VNWVTDSLHA KVTTFIPNHW 100
    HGDCIGGLGY LQRKGVQSYA NQMTIDLAKE KGLPVPEHGF TDSLTVSLDG 150
    MPLQCYYLGG GHATDNIVVW LPTENILFGG CMLKDNQATS IGNISDADVT 200
    AWPKTLDKVK AKFPSARYVV PGHGDYGGTE LIEHTKQIVN QYIESTSKP 249
    Length:249
    Mass (Da):27,257
    Last modified:May 1, 1992 - v1
    Checksum:i972B5A594DF5D40D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63556 Genomic DNA. Translation: AAA22904.1.
    M34831 Genomic DNA. Translation: AAA22907.1.
    PIRiA44999. A35263.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63556 Genomic DNA. Translation: AAA22904.1 .
    M34831 Genomic DNA. Translation: AAA22907.1 .
    PIRi A44999. A35263.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A7T X-ray 1.85 A/B 18-249 [» ]
    1A8T X-ray 2.55 A/B 18-249 [» ]
    1HLK X-ray 2.50 A/B 21-247 [» ]
    1KR3 X-ray 2.50 A/B 18-249 [» ]
    1ZNB X-ray 1.85 A/B 18-249 [» ]
    2BMI X-ray 2.00 A/B 18-249 [» ]
    2ZNB X-ray 2.15 A/B 18-249 [» ]
    3ZNB X-ray 2.70 A/B 18-249 [» ]
    4ZNB X-ray 2.65 A/B 18-249 [» ]
    ProteinModelPortali P25910.
    SMRi P25910. Positions 20-249.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P25910.
    ChEMBLi CHEMBL4840.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P25910.

    Miscellaneous databases

    EvolutionaryTracei P25910.

    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 class B beta-lactamase gene (ccrA) from Bacteroides fragilis TAL3636."
      Rasmussen B.A., Gluzman Y., Tally F.P.
      Antimicrob. Agents Chemother. 34:1590-1592(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: TAL3636.
    2. "Escherichia coli chromosomal mutations that permit direct cloning of the Bacteroides fragilis metallo-beta-lactamase gene, ccrA."
      Rasmussen B.A., Gluzman Y., Tally F.P.
      Mol. Microbiol. 5:1211-1219(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: TAL3636.
    3. "Sequencing the gene for an imipenem-cefoxitin-hydrolyzing enzyme (CfiA) from Bacteroides fragilis TAL2480 reveals strong similarity between CfiA and Bacillus cereus beta-lactamase II."
      Thompson J.S., Malamy M.H.
      J. Bacteriol. 172:2584-2593(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: TAL2480.
    4. "Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis."
      Concha N.O., Rasmusssen B.A., Bush K., Herzberg O.
      Structure 4:823-836(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
    5. "Crystal structures of the cadmium- and mercury-substituted metallo-beta-lactamase from Bacteroides fragilis."
      Concha N.O., Rasmussen B.A., Bush K., Herzberg O.
      Protein Sci. 6:2671-2676(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
    6. "X-ray structure of the ZnII beta-Lactamase from Bacteroides fragilis in an orthorhombic crystal form."
      Carfi A., Duee E., Soto R.-P., Galleni M., Frere J.-M., Dideberg O.
      Acta Crystallogr. D 54:47-57(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
      Strain: TAL2480.
    7. "Unanticipated inhibition of the metallo-beta-lactamase from Bacteroides fragilis by 4-morpholineethanesulfonic acid (MES): a crystallographic study at 1.85-A resolution."
      Fitzgerald P.M., Wu J.K., Toney J.H.
      Biochemistry 37:6791-6800(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
    8. "Structural consequences of the active site substitution Cys181 --> Ser in metallo-beta-lactamase from Bacteroides fragilis."
      Li Z., Rasmussen B.A., Herzberg O.
      Protein Sci. 8:249-252(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).

    Entry informationi

    Entry nameiBLAB_BACFG
    AccessioniPrimary (citable) accession number: P25910
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: May 1, 1992
    Last modified: October 1, 2014
    This is version 92 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

    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