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Protein

Carbapenem-hydrolyzing beta-lactamase BlaB-1

Gene

blaB1

Organism
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes penicillins, cephalosporins (including cefoxitin), carbapenems and 6-beta-iodopenicillanate.

Catalytic activityi

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

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi98 – 981Zinc 1By similarity
Metal bindingi100 – 1001Zinc 1By similarity
Metal bindingi102 – 1021Zinc 2By similarity
Metal bindingi161 – 1611Zinc 1By similarity
Metal bindingi180 – 1801Zinc 2By similarity
Metal bindingi222 – 2221Zinc 2By similarity

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

BioCyciMetaCyc:MONOMER-13428.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbapenem-hydrolyzing beta-lactamase BlaB-1 (EC:3.5.2.6)
Short name:
CHbetaL-1
Alternative name(s):
Class B carbapenemase BlaB-1
Gene namesi
Name:blaB1
Synonyms:blaB
OrganismiElizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Taxonomic identifieri238 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeElizabethkingia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22221 PublicationAdd
BLAST
Chaini23 – 249227Carbapenem-hydrolyzing beta-lactamase BlaB-1PRO_0000016949Add
BLAST

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
249
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 347Combined sources
Beta strandi37 – 4610Combined sources
Beta strandi49 – 6012Combined sources
Beta strandi63 – 686Combined sources
Helixi73 – 753Combined sources
Helixi76 – 8712Combined sources
Beta strandi91 – 955Combined sources
Beta strandi97 – 1004Combined sources
Turni101 – 1033Combined sources
Helixi107 – 1126Combined sources
Beta strandi116 – 1205Combined sources
Helixi121 – 1299Combined sources
Beta strandi136 – 1416Combined sources
Beta strandi143 – 1475Combined sources
Beta strandi150 – 1556Combined sources
Beta strandi159 – 1646Combined sources
Beta strandi167 – 1704Combined sources
Turni171 – 1744Combined sources
Beta strandi175 – 1795Combined sources
Helixi198 – 21114Combined sources
Turni212 – 2143Combined sources
Beta strandi216 – 2227Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M2XX-ray1.50A/B/C/D27-222[»]
ProteinModelPortaliO08498.
SMRiO08498. Positions 27-245.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO08498.

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.

O08498-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKKIKISLI LALGLTSLQA FGQENPDVKI EKLKDNLYVY TTYNTFNGTK
60 70 80 90 100
YAANAVYLVT DKGVVVIDCP WGEDKFKSFT DEIYKKHGKK VIMNIATHSH
110 120 130 140 150
DDRAGGLEYF GKIGAKTYST KMTDSILAKE NKPRAQYTFD NNKSFKVGKS
160 170 180 190 200
EFQVYYPGKG HTADNVVVWF PKEKVLVGGC IIKSADSKDL GYIGEAYVND
210 220 230 240
WTQSVHNIQQ KFSGAQYVVA GHDDWKDQRS IQHTLDLINE YQQKQKASN
Length:249
Mass (Da):28,144
Last modified:June 30, 1997 - v1
Checksum:i0F042B5126E338F6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X96858 Genomic DNA. Translation: CAA65601.1.
AF189298 Genomic DNA. Translation: AAF89154.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X96858 Genomic DNA. Translation: CAA65601.1.
AF189298 Genomic DNA. Translation: AAF89154.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M2XX-ray1.50A/B/C/D27-222[»]
ProteinModelPortaliO08498.
SMRiO08498. Positions 27-245.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

ChEMBLiCHEMBL1667692.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13428.

Miscellaneous databases

EvolutionaryTraceiO08498.

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. "Characterization and sequence of the Chryseobacterium (Flavobacterium) meningosepticum carbapenemase: a new molecular class B beta-lactamase showing a broad substrate profile."
    Rossolini G.M., Franceschini N., Riccio M.L., Mercuri P.S., Perilli M., Galleni M., Frere J.-M., Amicosante G.
    Biochem. J. 332:145-152(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-27, CHARACTERIZATION.
    Strain: ATCC 13254 / CCUG 4310 / CIP 6058 / LMG 12280 / NCTC 10585.
  2. "Molecular and biochemical heterogeneity of class B carbapenem-hydrolyzing beta-lactamases in Chryseobacterium meningosepticum."
    Bellais S., Aubert D., Naas T., Nordmann P.
    Antimicrob. Agents Chemother. 44:1878-1886(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: PINT.

Entry informationi

Entry nameiBLAB1_ELIME
AccessioniPrimary (citable) accession number: O08498
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 22, 2003
Last sequence update: June 30, 1997
Last modified: November 25, 2014
This is version 79 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

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.