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Protein

Metallo-beta-lactamase type 2

Gene

blm

Organism
Bacillus cereus
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. Active on cephalosporin and penicillin.1 Publication

Catalytic activityi

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

Cofactori

Zn2+5 PublicationsNote: Binds 2 Zn2+ ions per subunit. The enzyme can also function with only 1 Zn2+ ion (PubMed:9761898).5 Publications

Enzyme regulationi

Inhibited by captopril stereoisomers and iodoacetate (PubMed:3930467, PubMed:26482303). Also inhibited by chelating agents such as EDTA (PubMed:3930467).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi116Zinc 1; via tele nitrogen5 Publications1
Metal bindingi118Zinc 1; via pros nitrogen5 Publications1
Metal bindingi120Zinc 23 Publications1
Metal bindingi179Zinc 1; via tele nitrogen5 Publications1
Metal bindingi198Zinc 23 Publications1
Binding sitei201Substrate1 Publication1
Binding sitei210Substrate; via amide nitrogen2 Publications1
Metal bindingi240Zinc 2; via tele nitrogen3 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

BRENDAi3.5.2.6. 648.
SABIO-RKP04190.

Names & Taxonomyi

Protein namesi
Recommended name:
Metallo-beta-lactamase type 2Curated (EC:3.5.2.6By similarity)
Alternative name(s):
B2 metallo-beta-lactamaseCurated
Beta-lactamase II1 Publication
Cephalosporinase1 Publication
Metallo-beta-lactamase type II1 Publication
Metallothioprotein beta-lactamase II1 Publication
Penicillinase1 Publication
Zinc-requiring beta-lactamase II1 Publication
Gene namesi
Name:blm1 Publication
OrganismiBacillus cereus
Taxonomic identifieri1396 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 301 PublicationAdd BLAST30
ChainiPRO_000001694231 – 257Metallo-beta-lactamase type 2Add BLAST227

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1257
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi38 – 40Combined sources3
Beta strandi42 – 52Combined sources11
Beta strandi55 – 64Combined sources10
Beta strandi67 – 78Combined sources12
Beta strandi81 – 85Combined sources5
Helixi91 – 105Combined sources15
Beta strandi109 – 113Combined sources5
Beta strandi116 – 118Combined sources3
Helixi119 – 122Combined sources4
Helixi125 – 131Combined sources7
Beta strandi134 – 136Combined sources3
Helixi139 – 147Combined sources9
Beta strandi159 – 165Combined sources7
Beta strandi168 – 173Combined sources6
Beta strandi177 – 182Combined sources6
Beta strandi185 – 187Combined sources3
Turni189 – 191Combined sources3
Beta strandi194 – 197Combined sources4
Beta strandi212 – 214Combined sources3
Turni216 – 218Combined sources3
Helixi219 – 229Combined sources11
Beta strandi236 – 241Combined sources6
Helixi247 – 255Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4NQ4X-ray1.67A36-257[»]
4NQ5X-ray2.29A36-257[»]
4NQ6X-ray1.80A36-257[»]
4NQ7X-ray2.25A36-257[»]
4TYTX-ray1.80A31-257[»]
5FQAX-ray1.10A31-257[»]
5FQBX-ray1.90A31-257[»]
ProteinModelPortaliP04190.
SMRiP04190.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04190.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR001018. Beta-lactamase_class-B_CS.
IPR001279. Metallo-B-lactamas.
[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:
EMBLi
GenBanki
DDBJi
Links Updated
M11189 Genomic DNA. Translation: AAA22276.1.
PIRiA91806. PNBSU2.
RefSeqiWP_000742468.1. NZ_LOMO01000229.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11189 Genomic DNA. Translation: AAA22276.1.
PIRiA91806. PNBSU2.
RefSeqiWP_000742468.1. NZ_LOMO01000229.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4NQ4X-ray1.67A36-257[»]
4NQ5X-ray2.29A36-257[»]
4NQ6X-ray1.80A36-257[»]
4NQ7X-ray2.25A36-257[»]
4TYTX-ray1.80A31-257[»]
5FQAX-ray1.10A31-257[»]
5FQBX-ray1.90A31-257[»]
ProteinModelPortaliP04190.
SMRiP04190.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.5.2.6. 648.
SABIO-RKP04190.

Miscellaneous databases

EvolutionaryTraceiP04190.

Family and domain databases

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

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: November 2, 2016
This is version 117 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

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.