Soluble cytochrome b562 precursor

Contribute

Send feedback

Reviewed, UniProtKB/Swiss-Prot P0ABE7 (C562_ECOLX)

Last modified July 22, 2008. Version 27. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
Soluble cytochrome b562
Short name=Cytochrome b-562

Gene names

Name:

cybC

Organism

Escherichia coli

Taxonomic identifier

562 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Hide | Top

Protein attributes

Sequence length	128 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

Function	Electron-transport protein of unknown function.
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per molecule.
Subunit structure	Monomer.
Subcellular location	Periplasm.
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.

Hide | Top

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Periplasm
Domain	Signal
Ligand	Heme Iron Metal-binding
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
None. [Check GOA]

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Signal peptide

1 – 22

Chain

23 – 128

106

Soluble cytochrome b562

Sites

Metal binding

Iron (heme B axial ligand)

Metal binding

124

Iron (heme B axial ligand)

Secondary structure

128

Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P0ABE7-1 [UniParc].

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

FASTA

128

14,061

        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

Hide | Top

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: 1761034] [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: 8499452] [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: 4882876] [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: 368073] [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: 7031264] [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: 7723042] [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: 11914078] [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: 10393541] [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: 11669612] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

S74736 Genomic DNA. Translation: AAB20782.1.
X67290 Genomic DNA. Translation: CAA47706.1.
U14003 Genomic DNA. Translation: AAA97133.1. Different initiation.

PIR

CBEC62. S19544.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1APC	NMR	-	A	23-128	[»]
1LM3	X-ray	2.70	B/D	23-127	[»]
1M6T	X-ray	1.81	A	23-127	[»]
1QPU	NMR	-	A	23-128	[»]
1QQ3	NMR	-	A	23-128	[»]
1YYJ	NMR	-	A	23-127	[»]
1YYX	NMR	-	A	23-127	[»]
1YZA	NMR	-	A	23-127	[»]
1YZC	NMR	-	A	23-126	[»]
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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P0ABE7.

Phylogenomic databases

HOGENOM

P0ABE7.

Enzyme and pathway databases

BioCyc

EcoCyc:CYTOCHROME-B562-MON.

Family and domain databases

InterPro

IPR010980. Cyt_c_b562.
IPR009155. Cytochrome_b562.
IPR002197. HTH_Fis.
[Graphical view]

Gene3D

G3DSA:1.20.120.10. Cyt_c_b562. 1 hit.

Pfam

PF07361. Cytochrom_B562. 1 hit.
[Graphical view]

PIRSF

PIRSF000029. Cytochrome_b562. 1 hit.

PRINTS

PR01590. HTHFIS.

ProDom

P0ABE7.
[Graphical view] [Entries sharing at least one domain]

BLOCKS

Search...

Other Resources

BindingDB

P0ABE7.

LinkHub

P0ABE7.

ProtoNet

Search...

Hide | Top

Entry information

Entry name

C562_ECOLX

Accession

Primary (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:	July 22, 2008
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other Resources

Entry information

Relevant documents