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Protein

Beta-lactamase 1

Gene

blaY

Organism
Bacillus cereus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

This protein is a beta-lactamase with a substrate specificity for penicillins.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei91 – 911Acyl-ester intermediatePROSITE-ProRule annotation
Active sitei187 – 1871Proton acceptorBy similarity

GO - Molecular functioni

  1. beta-lactamase activity Source: UniProtKB-EC

GO - Biological processi

  1. beta-lactam antibiotic catabolic process Source: InterPro
  2. response to antibiotic Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antibiotic resistance

Enzyme and pathway databases

SABIO-RKP00809.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-lactamase 1 (EC:3.5.2.6)
Alternative name(s):
Beta-lactamase I
Penicillinase
Gene namesi
Name:blaY
OrganismiBacillus cereus
Taxonomic identifieri1396 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Add
BLAST
Chaini28 – 306279Beta-lactamase 1PRO_0000016970Add
BLAST

Interactioni

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CN9model-A80-104[»]
A258-270[»]
SMRiP00809. Positions 54-305.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni253 – 2553Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the class-A beta-lactamase family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR001466. Beta-lactam-related.
IPR012338. Beta-lactam/transpept-like.
IPR000871. Beta-lactam_class-A/D.
IPR023650. Beta-lactam_class-A_AS.
[Graphical view]
PfamiPF00144. Beta-lactamase. 1 hit.
[Graphical view]
PRINTSiPR00118. BLACTAMASEA.
SUPFAMiSSF56601. SSF56601. 1 hit.
PROSITEiPS00146. BETA_LACTAMASE_A. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00809-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MILKNKRMLK IGICVGILGL SITSLEAFTG ESLQVEAKEK TGQVKHKNQA
60 70 80 90 100
THKEFSQLEK KFDARLGVYA IDTGTNQTIS YRPNERFAFA STYKALAAGV
110 120 130 140 150
LLQQNSIDSL NEVITYTKED LVDYSPVTEK HVDTGMKLGE IAEAAVRSSD
160 170 180 190 200
NTAGNILFNK IGGPKGYEKA LRHMGDRITM SNRFETELNE AIPGDIRDTS
210 220 230 240 250
TAKAIATNLK AFTVGNALPA EKRKILTEWM KGNATGDKLI RAGIPTDWVV
260 270 280 290 300
GDKSGAGSYG TRNDIAVVWP PNSAPIIVLI SSKDEKEAIY NDQLIAEATK

VIVKGS
Length:306
Mass (Da):33,322
Last modified:July 21, 1986 - v1
Checksum:iF00F4DB9DB6D41AA
GO

Sequence cautioni

The sequence CAA26021.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA29819.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti273 – 2731S → R in CAA29819 (PubMed:3124817).Curated
Sequence conflicti278 – 2803VLI → IAIL in CAA29819 (PubMed:3124817).Curated
Sequence conflicti291 – 2922ND → DN in CAA29819 (PubMed:3124817).Curated
Sequence conflicti305 – 3062GS → ALR in CAA29819 (PubMed:3124817).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01990 Genomic DNA. Translation: CAA26021.1. Different initiation.
X01602 Genomic DNA. Translation: CAA25753.1.
X06599 Genomic DNA. Translation: CAA29819.1. Different initiation.
PIRiA01004. PNBSU.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01990 Genomic DNA. Translation: CAA26021.1. Different initiation.
X01602 Genomic DNA. Translation: CAA25753.1.
X06599 Genomic DNA. Translation: CAA29819.1. Different initiation.
PIRiA01004. PNBSU.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CN9model-A80-104[»]
A258-270[»]
SMRiP00809. Positions 54-305.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP00809.
ChEMBLiCHEMBL5732.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP00809.

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR001466. Beta-lactam-related.
IPR012338. Beta-lactam/transpept-like.
IPR000871. Beta-lactam_class-A/D.
IPR023650. Beta-lactam_class-A_AS.
[Graphical view]
PfamiPF00144. Beta-lactamase. 1 hit.
[Graphical view]
PRINTSiPR00118. BLACTAMASEA.
SUPFAMiSSF56601. SSF56601. 1 hit.
PROSITEiPS00146. BETA_LACTAMASE_A. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning and nucleotide sequence of the type I beta-lactamase gene from Bacillus cereus."
    Sloma A., Gross M.
    Nucleic Acids Res. 11:4997-5004(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 569/H / NCTC 9945.
  2. "Beta-lactamase I from Bacillus cereus. Structure and site-directed mutagenesis."
    Madgwick P.J., Waley S.G.
    Biochem. J. 248:657-662(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 569/H/9.
  3. "Bacillus cereus 569/H beta-lactamase I: cloning in Escherichia coli and signal sequence determination."
    Mezes P.S.F., Yang Y.Q., Hussain M., Lampen J.O.
    FEBS Lett. 161:195-200(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-75.
    Strain: 569/H / NCTC 9945.

Entry informationi

Entry nameiBLAC_BACCE
AccessioniPrimary (citable) accession number: P00809
Secondary accession number(s): P70876
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 1, 2015
This is version 81 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.