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P0ABE7

- C562_ECOLX

UniProt

P0ABE7 - C562_ECOLX

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Protein

Soluble cytochrome b562

Gene

cybC

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

Functioni

Electron-transport protein of unknown function.

Cofactori

Binds 1 heme B (iron-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-KW
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 – 4117
Helixi45 – 6218
Helixi68 – 703
Beta strandi71 – 733
Beta strandi75 – 773
Helixi78 – 10225
Helixi106 – 12722

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
S74736 Genomic DNA. Translation: AAB20782.1 .
X67290 Genomic DNA. Translation: CAA47706.1 .
U14003 Genomic DNA. Translation: AAA97133.1 . Different initiation.
PIRi S19544. CBEC62.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1APC NMR - A 23-128 [» ]
1LM3 X-ray 2.70 B/D 23-128 [» ]
1M6T X-ray 1.81 A 23-128 [» ]
1QPU NMR - A 23-128 [» ]
1QQ3 NMR - A 23-128 [» ]
256B X-ray 1.40 A/B 23-128 [» ]
2BC5 X-ray 2.25 A/B/C/D 23-128 [» ]
2QLA X-ray 2.90 A/B/C/D 23-128 [» ]
3C62 X-ray 1.87 A/B/C/D 23-128 [» ]
3C63 X-ray 1.75 A/B/C/D 23-128 [» ]
3DE8 X-ray 1.72 A/B/C/D 23-128 [» ]
3DE9 X-ray 2.04 A 23-128 [» ]
3FOO X-ray 2.40 A/B/C/D/E/F/G/H/I/J/K/L 23-128 [» ]
3FOP X-ray 3.00 A/B 23-128 [» ]
3HNI X-ray 2.35 A/B/C/D/E/F/G/H 23-128 [» ]
3HNJ X-ray 2.00 A/B/C/D 23-128 [» ]
3HNK X-ray 2.10 A/B 23-128 [» ]
3HNL X-ray 2.20 A/B 23-128 [» ]
3IQ5 X-ray 2.05 A/B/C/D 23-128 [» ]
3IQ6 X-ray 2.35 A/B/C/D/E/F/G/H 23-128 [» ]
3L1M X-ray 2.30 A 23-128 [» ]
3M15 X-ray 2.60 A/B/C 23-128 [» ]
3M4B X-ray 2.50 A/B/C/D 23-128 [» ]
3M4C X-ray 1.90 A/B/C/D 23-128 [» ]
3M79 X-ray 2.10 A/B/C/D/E/F/G/H 23-128 [» ]
3NMI X-ray 2.01 A/B/C/D/E/F 23-128 [» ]
3NMJ X-ray 3.10 A/B/C/D 23-128 [» ]
3NMK X-ray 2.80 A/B/C/D 23-128 [» ]
3TOL X-ray 2.00 A/B/C/D 23-128 [» ]
3TOM X-ray 2.30 A/B/C/D 23-128 [» ]
3U8P X-ray 2.75 A/B/C 23-128 [» ]
4EA3 X-ray 3.01 A/B 23-128 [» ]
4EIY X-ray 1.80 A 23-128 [» ]
4IAQ X-ray 2.80 A 23-128 [» ]
4IAR X-ray 2.70 A 23-128 [» ]
4IB4 X-ray 2.70 A 23-128 [» ]
4JE9 X-ray 2.12 A/B 23-128 [» ]
4JEA X-ray 1.22 A/B/C/D 23-128 [» ]
4JEB X-ray 2.30 A/B 23-128 [» ]
4JKV X-ray 2.45 A/B 23-127 [» ]
4L6R X-ray 3.30 A 23-128 [» ]
4N6H X-ray 1.80 A 23-128 [» ]
4NC3 X-ray 2.80 A 23-128 [» ]
4NTJ X-ray 2.62 A 23-128 [» ]
4O9R X-ray 3.20 A 23-128 [» ]
4OR2 X-ray 2.80 A/B 23-128 [» ]
4PXZ X-ray 2.50 A 23-128 [» ]
4PY0 X-ray 3.10 A 23-128 [» ]
4QIM X-ray 2.61 A 23-128 [» ]
4QIN X-ray 2.60 A 23-128 [» ]
ProteinModelPortali P0ABE7.
SMRi P0ABE7. Positions 23-128.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P0ABE7. 23 interactions.

Proteomic databases

PRIDEi P0ABE7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG3783.
HOGENOMi HOG000127440.

Miscellaneous databases

EvolutionaryTracei P0ABE7.

Family and domain databases

Gene3Di 1.20.120.10. 1 hit.
InterProi IPR009155. Cyt_b562.
IPR010980. Cyt_c/b562.
[Graphical view ]
Pfami PF07361. Cytochrom_B562. 1 hit.
[Graphical view ]
PIRSFi PIRSF000029. Cytochrome_b562. 1 hit.
SUPFAMi SSF47175. SSF47175. 1 hit.
ProtoNeti Search...

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: October 29, 2014
This is version 68 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