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Protein

Beta-lactamase type II

Gene

ccrA

Organism
Bacteroides fragilis
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Can hydrolyze carbapenem compounds.

Catalytic activityi

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

Cofactori

Zn2+Note: Binds 2 Zn2+ 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
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:
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 – 243Combined sources
Beta strandi25 – 328Combined sources
Beta strandi34 – 4613Combined sources
Turni47 – 493Combined sources
Beta strandi50 – 6112Combined sources
Beta strandi64 – 696Combined sources
Helixi74 – 8815Combined sources
Beta strandi91 – 966Combined sources
Beta strandi98 – 1014Combined sources
Helixi102 – 1054Combined sources
Helixi108 – 1136Combined sources
Beta strandi117 – 1215Combined sources
Helixi122 – 13110Combined sources
Beta strandi137 – 14812Combined sources
Beta strandi151 – 1566Combined sources
Beta strandi161 – 1633Combined sources
Beta strandi168 – 1703Combined sources
Turni172 – 1743Combined sources
Beta strandi176 – 1805Combined sources
Turni199 – 2013Combined sources
Helixi202 – 21211Combined sources
Beta strandi217 – 2248Combined sources
Helixi230 – 24617Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        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.

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Chemistry

BindingDBiP25910.
ChEMBLiCHEMBL4840.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP25910.

Miscellaneous databases

EvolutionaryTraceiP25910.

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]
ProtoNetiSearch...

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: November 26, 2014
This is version 93 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

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 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.