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P0ABE7

- C562_ECOLX

UniProt

P0ABE7 - C562_ECOLX

Protein

Soluble cytochrome b562

Gene

cybC

Organism
Escherichia coli
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. 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

    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

    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[»]
    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

    MRKSLLAILA VSSLVFSSAS FAADLEDNME TLNDNLKVIE KADNAAQVKD    50
    ALTKMRAAAL DAQKATPPKL EDKSPDSPEM KDFRHGFDIL VGQIDDALKL 100
    ANEGKVKEAQ AAAEQLKTTR NAYHQKYR 128
    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 [» ]
    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 1, 2014
    This is version 67 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