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Protein

Soluble cytochrome b562

Gene

cybC

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Electron-transport protein of unknown function.

Cofactori

heme bNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per molecule.

Redox potential

E0 is about +180 mV.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi29 – 291Iron (heme B axial ligand)
Metal bindingi124 – 1241Iron (heme B axial ligand)

GO - Molecular functioni

  1. electron carrier activity Source: InterPro
  2. heme binding Source: InterPro
  3. iron ion binding Source: InterPro

GO - Biological processi

  1. electron transport chain Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Soluble cytochrome b562
Short name:
Cytochrome b-562
Gene namesi
Name:cybC
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Subcellular locationi

Periplasm 1 Publication

GO - Cellular componenti

  1. periplasmic space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22221 PublicationAdd
BLAST
Chaini23 – 128106Soluble cytochrome b562PRO_0000003640Add
BLAST

Proteomic databases

PRIDEiP0ABE7.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

IntActiP0ABE7. 23 interactions.

Structurei

Secondary structure

1
128
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi25 – 4117Combined sources
Helixi45 – 6218Combined sources
Helixi68 – 703Combined sources
Beta strandi71 – 733Combined sources
Beta strandi75 – 773Combined sources
Helixi78 – 10225Combined sources
Helixi106 – 12722Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1APCNMR-A23-128[»]
1LM3X-ray2.70B/D23-128[»]
1M6TX-ray1.81A23-128[»]
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/B23-128[»]
4EIYX-ray1.80A23-128[»]
4IAQX-ray2.80A23-128[»]
4IARX-ray2.70A23-128[»]
4IB4X-ray2.70A23-128[»]
4JE9X-ray2.12A/B23-128[»]
4JEAX-ray1.22A/B/C/D23-128[»]
4JEBX-ray2.30A/B23-128[»]
4JKVX-ray2.45A/B23-127[»]
4L6RX-ray3.30A23-128[»]
4N6HX-ray1.80A23-128[»]
4NC3X-ray2.80A23-128[»]
4NTJX-ray2.62A23-128[»]
4O9RX-ray3.20A23-128[»]
4OR2X-ray2.80A/B23-128[»]
4PXZX-ray2.50A23-128[»]
4PY0X-ray3.10A23-128[»]
4QIMX-ray2.61A23-128[»]
4QINX-ray2.60A23-128[»]
ProteinModelPortaliP0ABE7.
SMRiP0ABE7. Positions 23-128.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ABE7.

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome b562 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3783.
HOGENOMiHOG000127440.

Family and domain databases

Gene3Di1.20.120.10. 1 hit.
InterProiIPR009155. Cyt_b562.
IPR010980. Cyt_c/b562.
[Graphical view]
PfamiPF07361. Cytochrom_B562. 1 hit.
[Graphical view]
PIRSFiPIRSF000029. Cytochrome_b562. 1 hit.
SUPFAMiSSF47175. SSF47175. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P0ABE7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRKSLLAILA VSSLVFSSAS FAADLEDNME TLNDNLKVIE KADNAAQVKD
60 70 80 90 100
ALTKMRAAAL DAQKATPPKL EDKSPDSPEM KDFRHGFDIL VGQIDDALKL
110 120
ANEGKVKEAQ AAAEQLKTTR NAYHQKYR
Length:128
Mass (Da):14,061
Last modified:October 25, 2005 - v1
Checksum:iD7D822AC8FEED751
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S74736 Genomic DNA. Translation: AAB20782.1.
X67290 Genomic DNA. Translation: CAA47706.1.
U14003 Genomic DNA. Translation: AAA97133.1. Different initiation.
PIRiS19544. CBEC62.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S74736 Genomic DNA. Translation: AAB20782.1.
X67290 Genomic DNA. Translation: CAA47706.1.
U14003 Genomic DNA. Translation: AAA97133.1. Different initiation.
PIRiS19544. CBEC62.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1APCNMR-A23-128[»]
1LM3X-ray2.70B/D23-128[»]
1M6TX-ray1.81A23-128[»]
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/B23-128[»]
4EIYX-ray1.80A23-128[»]
4IAQX-ray2.80A23-128[»]
4IARX-ray2.70A23-128[»]
4IB4X-ray2.70A23-128[»]
4JE9X-ray2.12A/B23-128[»]
4JEAX-ray1.22A/B/C/D23-128[»]
4JEBX-ray2.30A/B23-128[»]
4JKVX-ray2.45A/B23-127[»]
4L6RX-ray3.30A23-128[»]
4N6HX-ray1.80A23-128[»]
4NC3X-ray2.80A23-128[»]
4NTJX-ray2.62A23-128[»]
4O9RX-ray3.20A23-128[»]
4OR2X-ray2.80A/B23-128[»]
4PXZX-ray2.50A23-128[»]
4PY0X-ray3.10A23-128[»]
4QIMX-ray2.61A23-128[»]
4QINX-ray2.60A23-128[»]
ProteinModelPortaliP0ABE7.
SMRiP0ABE7. Positions 23-128.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP0ABE7. 23 interactions.

Proteomic databases

PRIDEiP0ABE7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG3783.
HOGENOMiHOG000127440.

Miscellaneous databases

EvolutionaryTraceiP0ABE7.

Family and domain databases

Gene3Di1.20.120.10. 1 hit.
InterProiIPR009155. Cyt_b562.
IPR010980. Cyt_c/b562.
[Graphical view]
PfamiPF07361. Cytochrom_B562. 1 hit.
[Graphical view]
PIRSFiPIRSF000029. Cytochrome_b562. 1 hit.
SUPFAMiSSF47175. SSF47175. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiC562_ECOLX
AccessioniPrimary (citable) accession number: P0ABE7
Secondary accession number(s): P00192, P76805, Q8XCE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 25, 2005
Last modified: January 7, 2015
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.Curated

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.