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Protein

Metallo-beta-lactamase type 2

Gene

ccrA

Organism
Bacteroides fragilis
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.3 Publications

Catalytic activityi

A beta-lactam + H2O = a substituted beta-amino acid.1 Publication

Cofactori

Zn2+8 PublicationsNote: Binds 2 Zn2+ ions per subunit. It can also bind Cd2+ and Co2+ to a lesser extent (PubMed:9416622).7 Publications

Enzyme regulationi

Competitively inhibited by 4-morpholineethanesulfonic acid (MES), SB236050 and biphenyl tetrazoles (BPTs) (PubMed:9578564, PubMed:9545432, PubMed:12019104). Also inhibited by chelating agents such as EDTA and 1,10-phenanthroline (PubMed:9712862). CcrA is not susceptible to inactivation by the beta-lactamase-blocking agents clavulanic acid or tazobactam (PubMed:2121094, PubMed:2110145).6 Publications

Kineticsi

Kcat is 225.7 sec(-1) for lactamase activity with nitrocefin as substrate (with zinc ions at pH 7 and 25 degrees Celsius). Kcat is 107.6 sec(-1) for lactamase activity with nitrocefin as substrate (with cobalt ions at pH 7 and 25 degrees Celsius).1 Publication

Manual assertion based on experiment ini

  1. KM=7.1 µM for nitrocefin (with zinc ions at pH 7 and 25 degrees Celsius)1 Publication
  2. KM=14 µM for nitrocefin (with cobalt ions at pH 7 and 25 degrees Celsius)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi99Zinc 1; via tele nitrogen7 Publications1
    Metal bindingi101Zinc 1; via pros nitrogen7 Publications1
    Metal bindingi103Zinc 26 Publications1
    Metal bindingi162Zinc 1; via tele nitrogen7 Publications1
    Metal bindingi181Zinc 26 Publications1
    Binding sitei184Substrate1 Publication1
    Binding sitei193Substrate; via amide nitrogen3 Publications1
    Metal bindingi223Zinc 2; via tele nitrogen6 Publications1

    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

    SABIO-RKP25910.

    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 II1 Publication
    Carbapenem and cephamycin resistance1 Publication
    Short name:
    CCRA1 Publication
    CephalosporinaseCurated
    Imipenem-cefoxitin hydrolyzing enzyme1 Publication
    Metallo-beta-lactamase type II1 Publication
    PenicillinaseCurated
    Zinc-requiring beta-lactamase1 Publication
    Gene namesi
    Name:ccrA1 Publication
    Synonyms:cfiA1 Publication
    OrganismiBacteroides fragilis
    Taxonomic identifieri817 [NCBI]
    Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

    Subcellular locationi

    • Periplasm 1 Publication

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Periplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi181C → S: The overall structure of the mutant is the same as that of the wild-type, however the site of the second zinc ion is unoccupied. 1 Publication1

    Chemistry databases

    ChEMBLiCHEMBL4840.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 18Sequence analysis2 PublicationsAdd BLAST18
    ChainiPRO_000001694519 – 249Metallo-beta-lactamase type 2Add BLAST231

    Interactioni

    Subunit structurei

    Monomer.4 Publications

    Protein-protein interaction databases

    STRINGi457424.BFAG_03627.

    Chemistry databases

    BindingDBiP25910.

    Structurei

    Secondary structure

    1249
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi22 – 24Combined sources3
    Beta strandi25 – 32Combined sources8
    Beta strandi34 – 46Combined sources13
    Turni47 – 49Combined sources3
    Beta strandi50 – 61Combined sources12
    Beta strandi64 – 69Combined sources6
    Helixi74 – 88Combined sources15
    Beta strandi91 – 96Combined sources6
    Beta strandi98 – 101Combined sources4
    Helixi102 – 105Combined sources4
    Helixi108 – 113Combined sources6
    Beta strandi117 – 121Combined sources5
    Helixi122 – 131Combined sources10
    Beta strandi137 – 148Combined sources12
    Beta strandi151 – 156Combined sources6
    Beta strandi161 – 163Combined sources3
    Beta strandi168 – 170Combined sources3
    Turni172 – 174Combined sources3
    Beta strandi176 – 180Combined sources5
    Turni199 – 201Combined sources3
    Helixi202 – 212Combined sources11
    Beta strandi217 – 224Combined sources8
    Helixi230 – 246Combined sources17

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP25910.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiENOG4107YH7. Bacteria.
    ENOG410ZW82. LUCA.

    Family and domain databases

    Gene3Di3.60.15.10. 1 hit.
    InterProiIPR001018. Beta-lactamase_class-B_CS.
    IPR001279. Metallo-B-lactamas.
    [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

            10         20         30         40         50
    MKTVFILISM LFPVAVMAQK SVKISDDISI TQLSDKVYTY VSLAEIEGWG
    60 70 80 90 100
    MVPSNGMIVI NNHQAALLDT PINDAQTEML VNWVTDSLHA KVTTFIPNHW
    110 120 130 140 150
    HGDCIGGLGY LQRKGVQSYA NQMTIDLAKE KGLPVPEHGF TDSLTVSLDG
    160 170 180 190 200
    MPLQCYYLGG GHATDNIVVW LPTENILFGG CMLKDNQATS IGNISDADVT
    210 220 230 240
    AWPKTLDKVK AKFPSARYVV PGHGDYGGTE LIEHTKQIVN QYIESTSKP
    Length:249
    Mass (Da):27,257
    Last modified:May 1, 1992 - v1
    Checksum:i972B5A594DF5D40D
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M63556 Genomic DNA. Translation: AAA22904.1.
    M34831 Genomic DNA. Translation: AAA22907.1.
    PIRiA44999. A35263.
    RefSeqiWP_005808062.1. NZ_JPHS01000286.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M63556 Genomic DNA. Translation: AAA22904.1.
    M34831 Genomic DNA. Translation: AAA22907.1.
    PIRiA44999. A35263.
    RefSeqiWP_005808062.1. NZ_JPHS01000286.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi457424.BFAG_03627.

    Chemistry databases

    BindingDBiP25910.
    ChEMBLiCHEMBL4840.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    eggNOGiENOG4107YH7. Bacteria.
    ENOG410ZW82. LUCA.

    Enzyme and pathway databases

    SABIO-RKP25910.

    Miscellaneous databases

    EvolutionaryTraceiP25910.

    Family and domain databases

    Gene3Di3.60.15.10. 1 hit.
    InterProiIPR001018. Beta-lactamase_class-B_CS.
    IPR001279. Metallo-B-lactamas.
    [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 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: November 2, 2016
    This is version 104 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

    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.