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BACCE:BLA2

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Species (Taxon ID) Bacillus cereus. (1396)
Gene Name(s) blm
Protein Name(s) Beta-lactamase 2

Beta-lactamase II Cephalosporinase Penicillinase

External Links
UniProt P04190
EMBL M11189
PIR A91806
PDB 1BC2
1BMC
1BVT
1DXK
1MQO
2BC2
2BFK
2BFL
2BFZ
2BG2
2BG6
2BG7
2BG8
2BGA
2M5C
2M5D
2NXA
2NYP
2NZE
2NZF
2UYX
3BC2
3FCZ
3I0V
3I11
3I13
3I14
3I15
3KNR
3KNS
4C09
4C1C
4C1H
4NQ4
4NQ5
4NQ6
4NQ7
4TYT
PDBsum 1BC2
1BMC
1BVT
1DXK
1MQO
2BC2
2BFK
2BFL
2BFZ
2BG2
2BG6
2BG7
2BG8
2BGA
2M5C
2M5D
2NXA
2NYP
2NZE
2NZF
2UYX
3BC2
3FCZ
3I0V
3I11
3I13
3I14
3I15
3KNR
3KNS
4C09
4C1C
4C1H
4NQ4
4NQ5
4NQ6
4NQ7
4TYT
ProteinModelPortal P04190
SMR P04190
BRENDA 3.5.2.6
SABIO-RK P04190
EvolutionaryTrace P04190
GO GO:0008800
GO:0008270
GO:0017001
GO:0046677
Gene3D 3.60.15.10
InterPro IPR001279
IPR001018
Pfam PF00753
SMART SM00849
SUPFAM SSF56281
PROSITE PS00743
PS00744

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

enables

GO:0008270

zinc ion binding

PMID:7588620[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

PMID:26482303[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0017001

antibiotic catabolic process

PMID:3930467[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008800

beta-lactamase activity

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P25910

F

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001018

F

Seeded From UniProt

complete

enables

GO:0008800

beta-lactamase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001018

F

Seeded From UniProt

complete

involved_in

GO:0017001

antibiotic catabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001018

P

Seeded From UniProt

complete

enables

GO:0008800

beta-lactamase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.5.2.6

F

Seeded From UniProt

complete

involved_in

GO:0046677

response to antibiotic

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0046

P

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

part_of

GO:0042597

periplasmic space

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0574
UniProtKB-SubCell:SL-0200

C

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Carfi, A et al. (1995) The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold. EMBO J. 14 4914-21 PubMed GONUTS page
  2. Brem, J et al. (2016) Structural Basis of Metallo-β-Lactamase Inhibition by Captopril Stereoisomers. Antimicrob. Agents Chemother. 60 142-50 PubMed GONUTS page
  3. Hussain, M et al. (1985) Cloning and sequencing of the metallothioprotein beta-lactamase II gene of Bacillus cereus 569/H in Escherichia coli. J. Bacteriol. 164 223-9 PubMed GONUTS page