P0ABE7 (C562_ECOLX) Reviewed, UniProtKB/Swiss-Prot

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

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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

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 process	Electron transport Transport
Cellular component	Periplasm
Domain	Signal
Ligand	Heme Iron Metal-binding
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	electron 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Ref.3

Chain

23 – 128

106

Soluble cytochrome b562

PRO_0000003640

Sites

Metal binding

29

1

Iron (heme B axial ligand)

Metal binding

124

1

Iron (heme B axial ligand)

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

128

Helix Strand Turn

Details...

Helix

25 – 41

17

Helix

45 – 62

18

Helix

68 – 70

3

Beta strand

71 – 73

3

Helix

78 – 102

25

Helix

106 – 113

8

Helix

115 – 127

13

Sequences

	Sequence		Length	Mass (Da)
	P0ABE7 [UniParc]. Last modified October 25, 2005. Version 1. Checksum: D7D822AC8FEED751	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

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.

PIR

CBEC62. S19544.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
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	23-127	[»]
4IAQ	X-ray	2.80	A	23-127	[»]

ProteinModelPortal

P0ABE7.

SMR

P0ABE7. Positions 23-128.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0ABE7. 23 interactions.

Proteomic databases

PRIDE

P0ABE7.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

eggNOG

COG3783.

HOGENOM

HOG000127440.

Enzyme and pathway databases

BioCyc

EcoCyc:CYTOCHROME-B562-MONOMER.

Family and domain databases

Gene3D

1.20.120.10. 1 hit.

InterPro

IPR009155. Cyt_b562.
IPR010980. Cyt_c/b562.
[Graphical view]

Pfam

PF07361. Cytochrom_B562. 1 hit.
[Graphical view]

PIRSF

PIRSF000029. Cytochrome_b562. 1 hit.

SUPFAM

SSF47175. Cyt_c_b562. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P0ABE7.

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:	May 1, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program