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P04190

- BLA2_BACCE

UniProt

P04190 - BLA2_BACCE

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Protein

Beta-lactamase 2

Gene

blm

Organism
Bacillus cereus
Status
Reviewed - 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

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
Complete GO annotation...

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[»]
4C09X-ray1.20A31-257[»]
4C1CX-ray1.18A31-257[»]
4C1HX-ray1.10A31-257[»]
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

        10         20         30         40         50
MKKNTLLKVG LCVGLLGTIQ FVSTISSVQA SQKVEKTVIK NETGTISISQ
60 70 80 90 100
LNKNVWVHTE LGSFNGEAVP SNGLVLNTSK GLVLVDSSWD DKLTKELIEM
110 120 130 140 150
VEKKFQKRVT DVIITHAHAD RIGGIKTLKE RGIKAHSTAL TAELAKKNGY
160 170 180 190 200
EEPLGDLQTV TNLKFGNMKV ETFYPGKGHT EDNIVVWLPQ YNILVGGCLV
210 220 230 240 250
KSTSAKDLGN VADAYVNEWS TSIENVLKRY RNINAVVPGH GEVGDKGLLL

HTLDLLK
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 [» ]
4C09 X-ray 1.20 A 31-257 [» ]
4C1C X-ray 1.18 A 31-257 [» ]
4C1H X-ray 1.10 A 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 29, 2014
This is version 101 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