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P0ABE7 (C562_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Soluble cytochrome b562

Short name=Cytochrome b-562
Gene names
Name:cybC
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length128 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Electron-transport protein of unknown function.

Cofactor

Binds 1 heme B (iron-protoporphyrin IX) group per molecule.

Subunit structure

Monomer. Ref.4

Subcellular location

Periplasm Ref.1.

Sequence similarities

Belongs to the cytochrome b562 family.

Caution

In strains K / NM522 and K12 / MG1655 the cybC gene has a 26 bp deletion and lacks the first 7 amino acids. It is not translated in those strains.

Biophysicochemical properties

Redox potential:

E0 is about +180 mV.

Sequence caution

The sequence AAA97133.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processElectron transport
Transport
   Cellular componentPeriplasm
   DomainSignal
   LigandHeme
Iron
Metal-binding
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processelectron transport chain

Inferred from electronic annotation. Source: InterPro

   Cellular_componentperiplasmic space

Inferred from direct assay. Source: EcoCyc

   Molecular_functionelectron carrier activity

Inferred from electronic annotation. Source: InterPro

heme binding

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.3
Chain23 – 128106Soluble cytochrome b562
PRO_0000003640

Sites

Metal binding291Iron (heme B axial ligand)
Metal binding1241Iron (heme B axial ligand)

Secondary structure

............. 128
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0ABE7 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: D7D822AC8FEED751

FASTA12814,061
        10         20         30         40         50         60 
MRKSLLAILA VSSLVFSSAS FAADLEDNME TLNDNLKVIE KADNAAQVKD ALTKMRAAAL 

        70         80         90        100        110        120 
DAQKATPPKL EDKSPDSPEM KDFRHGFDIL VGQIDDALKL ANEGKVKEAQ AAAEQLKTTR 


NAYHQKYR 

« Hide

References

[1]"Cloning and expression of the gene encoding the soluble cytochrome b562 of Escherichia coli."
Nikkila H., Gennis R.B., Sligar S.G.
Eur. J. Biochem. 202:309-313(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
Strain: B.
[2]"PCR cloning, sequence analysis and expression of the cybC genes encoding soluble cytochrome b-562 from Escherichia coli B strain OP7 and K strain NM522."
Trower M.K.
Biochim. Biophys. Acta 1143:109-111(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: B / OP7 and K / NM522.
[3]"The amino acid sequence of cytochrome b562 of Escherichia coli."
Itagaki E., Hager L.P.
Biochem. Biophys. Res. Commun. 32:1013-1019(1968) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-128.
Strain: B.
[4]"The structure of cytochrome b562 from Escherichia coli at 2.5-A resolution."
Mathews F.S., Bethge P.H., Czerwinski E.W.
J. Biol. Chem. 254:1699-1706(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SUBUNIT.
[5]"Improvement of the 2.5-A resolution model of cytochrome b562 by redetermining the primary structure and using molecular graphics."
Lederer F., Glatigny A., Bethge P.H., Bellamy H.D., Mathews F.S.
J. Mol. Biol. 148:427-448(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SEQUENCE REVISION.
[6]"Refined structure of cytochrome b562 from Escherichia coli at 1.4-A resolution."
Hamada K., Bethge P.H., Mathews F.S.
J. Mol. Biol. 247:947-962(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
[7]"A multigeneration analysis of cytochrome b562 redox variants: evolutionary strategies for modulating redox potential revealed using a library approach."
Springs S.L., Bass S.E., Bowman G., Nodelman I., Schutt C.E., McLendon G.L.
Biochemistry 41:4321-4328(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF F83I/F87Y/R128L VARIANT.
[8]"The solution structure of oxidized Escherichia coli cytochrome b562."
Arnesano F., Banci L., Bertini I., Faraone-Mennella J., Rosato A., Barker P.D., Fersht A.R.
Biochemistry 38:8657-8670(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[9]"(15)N backbone dynamics of ferricytochrome b(562): comparison with the reduced protein and the R98C variant."
Assfalg M., Banci L., Bertini I., Ciofi-Baffoni S., Barker P.D.
Biochemistry 40:12761-12771(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S74736 Genomic DNA. Translation: AAB20782.1.
X67290 Genomic DNA. Translation: CAA47706.1.
U14003 Genomic DNA. Translation: AAA97133.1. Different initiation.
PIRCBEC62. S19544.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1APCNMR-A23-128[»]
1LM3X-ray2.70B/D23-127[»]
1M6TX-ray1.81A23-127[»]
1QPUNMR-A23-128[»]
1QQ3NMR-A23-128[»]
256BX-ray1.40A/B23-128[»]
2BC5X-ray2.25A/B/C/D23-128[»]
2QLAX-ray2.90A/B/C/D23-128[»]
3C62X-ray1.87A/B/C/D23-128[»]
3C63X-ray1.75A/B/C/D23-128[»]
3DE8X-ray1.72A/B/C/D23-128[»]
3DE9X-ray2.04A23-128[»]
3FOOX-ray2.40A/B/C/D/E/F/G/H/I/J/K/L23-128[»]
3FOPX-ray3.00A/B23-128[»]
3HNIX-ray2.35A/B/C/D/E/F/G/H23-128[»]
3HNJX-ray2.00A/B/C/D23-128[»]
3HNKX-ray2.10A/B23-128[»]
3HNLX-ray2.20A/B23-128[»]
3IQ5X-ray2.05A/B/C/D23-128[»]
3IQ6X-ray2.35A/B/C/D/E/F/G/H23-128[»]
3L1MX-ray2.30A23-128[»]
3M15X-ray2.60A/B/C23-128[»]
3M4BX-ray2.50A/B/C/D23-128[»]
3M4CX-ray1.90A/B/C/D23-128[»]
3M79X-ray2.10A/B/C/D/E/F/G/H23-128[»]
3NMIX-ray2.01A/B/C/D/E/F23-128[»]
3NMJX-ray3.10A/B/C/D23-128[»]
3NMKX-ray2.80A/B/C/D23-128[»]
3TOLX-ray2.00A/B/C/D23-128[»]
3TOMX-ray2.30A/B/C/D23-128[»]
3U8PX-ray2.75A/B/C23-128[»]
4EA3X-ray3.01A/B23-127[»]
4EIYX-ray1.80A23-128[»]
4IAQX-ray2.80A23-127[»]
4IARX-ray2.70A23-128[»]
4IB4X-ray2.70A22-128[»]
4JE9X-ray2.12A/B23-122[»]
4JEAX-ray1.22A/B/C/D23-122[»]
4JEBX-ray2.30A/B23-122[»]
4JKVX-ray2.45A/B23-127[»]
4L6RX-ray3.30A23-128[»]
4N6HX-ray1.80A23-128[»]
4NC3X-ray2.80A23-128[»]
4O9RX-ray3.20A23-128[»]
ProteinModelPortalP0ABE7.
SMRP0ABE7. Positions 23-128.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP0ABE7. 23 interactions.

Proteomic databases

PRIDEP0ABE7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG3783.
HOGENOMHOG000127440.

Enzyme and pathway databases

BioCycEcoCyc:CYTOCHROME-B562-MONOMER.

Family and domain databases

Gene3D1.20.120.10. 1 hit.
InterProIPR009155. Cyt_b562.
IPR010980. Cyt_c/b562.
[Graphical view]
PfamPF07361. Cytochrom_B562. 1 hit.
[Graphical view]
PIRSFPIRSF000029. Cytochrome_b562. 1 hit.
SUPFAMSSF47175. SSF47175. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0ABE7.

Entry information

Entry nameC562_ECOLX
AccessionPrimary (citable) accession number: P0ABE7
Secondary accession number(s): P00192, P76805, Q8XCE3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 25, 2005
Last modified: April 16, 2014
This is version 64 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references