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A1A9S3 (EFEB_ECOK1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Deferrochelatase/peroxidase EfeB

EC=1.11.1.-
Gene names
Name:efeB
Ordered Locus Names:Ecok1_09190
OrganismEscherichia coli O1:K1 / APEC [Complete proteome] [HAMAP]
Taxonomic identifier405955 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length423 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in the recovery of exogenous heme iron. Extracts iron from heme while preserving the tetrapyrrol ring intact By similarity.

Cofactor

Binds 1 heme B (iron-protoporphyrin IX) group non-covalently per subunit By similarity.

Subunit structure

Homodimer. Part of a ferrous iron transporter composed of EfeU, EfeO and EfeB By similarity.

Subcellular location

Periplasm By similarity.

Post-translational modification

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.

Sequence similarities

Belongs to the DyP-type peroxidase family. EfeB subfamily.

Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular_componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionheme binding

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: InterPro

peroxidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535Tat-type signal Potential
Chain36 – 423388Deferrochelatase/peroxidase EfeB
PRO_0000278545

Regions

Region236 – 2383Heme binding By similarity
Region334 – 3363Heme binding By similarity

Sites

Metal binding3291Iron (heme proximal ligand); via tele nitrogen By similarity
Binding site3471Heme By similarity

Sequences

Sequence LengthMass (Da)Tools
A1A9S3 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 9EB660519206CD2E

FASTA42346,654
        10         20         30         40         50         60 
MQYEDENGVN EPSRRRLLKG IGALALAGSC PVAHAQKTQS APGTLSPDAR NEKQPFYGEH 

        70         80         90        100        110        120 
QAGILTPQQA AMMLVAFDVL ASDKADLERL FRLLTQRFAF LTQGGAAPET PNPRLPPLDS 

       130        140        150        160        170        180 
GILGGYIAPD NLTITLSVGH SLFDERFGLA PQMPKKLQKM TRFPNDSLDA ALCHGDVLLQ 

       190        200        210        220        230        240 
ICANTQDTVI HALRDIIKHT PDLLSVRWKR EGFISDHAAR SKGKETPINL LGFKDGTANP 

       250        260        270        280        290        300 
DSQNDKLMQK VVWVTADQQE PAWTIGGSYQ AVRLIQFRVE FWDRTPLKEQ QTIFGRDKQT 

       310        320        330        340        350        360 
GAPLGMLHEH DVPDYASDPE GKVIALDSHI RLANPRTAES ESSLMLRRGY SYSLGVTNSG 

       370        380        390        400        410        420 
QLDMGLLFVC YQHDLEKGFL TVQKRLNGEA LEEYVKPIGG GYFFALSGVK DANDYLGSAL 


LRV 

« Hide

References

[1]"The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7 shares strong similarities with human extraintestinal pathogenic E. coli genomes."
Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.
J. Bacteriol. 189:3228-3236(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000468 Genomic DNA. Translation: ABJ00413.1.
RefSeqYP_852127.1. NC_008563.1.

3D structure databases

ProteinModelPortalA1A9S3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING405955.APECO1_110.

Protein family/group databases

PeroxiBase5878. EcoDyPrx01_APECO1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ00413; ABJ00413; APECO1_110.
GeneID4495215.
KEGGecv:APECO1_110.
PATRIC18213474. VBIEscCol127180_1024.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2837.
KOK16301.
OMALPPMDSG.
OrthoDBEOG6F55G9.

Family and domain databases

InterProIPR011008. Dimeric_a/b-barrel.
IPR006314. Dyp_peroxidase.
IPR006313. Tat_enzyme.
IPR006311. TAT_signal.
[Graphical view]
PfamPF04261. Dyp_perox. 1 hit.
[Graphical view]
SUPFAMSSF54909. SSF54909. 1 hit.
TIGRFAMsTIGR01413. Dyp_perox_fam. 1 hit.
TIGR01412. tat_substr_1. 1 hit.
PROSITEPS51404. DYP_PEROXIDASE. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameEFEB_ECOK1
AccessionPrimary (citable) accession number: A1A9S3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families