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Reviewed, UniProtKB/Swiss-Prot Q44056 (BLA1_AERHY)

Last modified September 22, 2009. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Beta-lactamase AER-1
    EC=3.5.2.6
Alternative name(s):
    Penicillinase
Gene names
Name: aer1
OrganismAeromonas hydrophila
Taxonomic identifier644 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas

Protein attributes

Sequence length304 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Hydrolyzes carbenicillin. Methicillin and oxacillin are weakly hydrolyzed.

Catalytic activity

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

Sequence similarities

Belongs to the class-A beta-lactamase family.

Ontologies

Keywords
   Biological processAntibiotic resistance
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
   Technical termTransposable element
Gene Ontology (GO)
   Biological processbeta-lactam antibiotic catabolic process

Inferred from electronic annotation. Source: InterPro

response to antibiotic

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionbeta-lactamase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3737 Potential
Chain38 – 304267Beta-lactamase AER-1
PRO_0000017048

Regions

Region248 – 2503Substrate binding By similarity

Sites

Active site831Acyl-ester intermediate By similarity

Amino acid modifications

Disulfide bond90 ↔ 137 Potential

Sequences

Sequence LengthMass (Da)Tools
Q44056-1 [UniParc].

Last modified August 1, 1998. Version 2.
Checksum: 66AD56ED45D02A41

FASTA30432,428
        10         20         30         40         50         60 
MYVLSVEKPT LRNKFAAGIG VVLVCVVASF IPTPVFALDT TKLIQAVQSE ESALHARVGM 

        70         80         90        100        110        120 
TVFDSNTGTT WNYRGDERFP LNSTHKTFSC AALLAKVDGK SLSLGQSVSI SKEMLVTYSP 

       130        140        150        160        170        180 
ITEKSLSPET VTFGKICQAA VSYSDNTAAN VVFDAIGGAT GFNAYMRSIG DEETQLDRKE 

       190        200        210        220        230        240 
PELNEGTPGD VRDTTTPNAM VNSLRKILLG DALSASSRSQ LTQWMLDDQV AGALLRASLP 

       250        260        270        280        290        300 
SDWKIADKTG AGGYGSRSIV AVIWPPSKQP LVVGIYITQT KASMQASNQA IARIGVVLKD 


TVAP 

« Hide

References

[1]"Structure of CARB-4 and AER-1 carbenicillin-hydrolyzing beta-lactamases."
Sanschagrin F., Bejaoui N., Levesque R.C.
Antimicrob. Agents Chemother. 42:1966-1972(1998) [PubMed: 9687391] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: VL7711.
Transposon: Omega7711.

Cross-references

Sequence databases

U14748 Genomic DNA. Translation: AAC09015.1.

3D structure databases

HSSPHSSP built from PDB template 1JTG based on UniProtKB P00810.
ModBaseSearch...

Enzyme and pathway databases

BRENDA3.5.2.6. 3060.

Family and domain databases

InterProIPR001466. Beta_lactamase-related.
IPR000871. Beta_lactamase_A/D.
[Graphical view]
PfamPF00144. Beta-lactamase. 1 hit.
[Graphical view]
PRINTSPR00118. BLACTAMASEA.
PROSITEPS00146. BETA_LACTAMASE_A. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBLA1_AERHY
AccessionPrimary (citable) accession number: Q44056
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: September 22, 2009
This is version 45 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents