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P33226 (TORC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytochrome c-type protein TorC
Gene names
Name:torC
Ordered Locus Names:b0996, JW0981
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length390 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Part of the anaerobic respiratory chain of trimethylamine-N-oxide reductase TorA. Acts by transferring electrons from the membranous menaquinones to TorA. This transfer probably involves an electron transfer pathway from menaquinones to the N-terminal domain of TorC, then from the N-terminus to the C-terminus, and finally to TorA. TorC apocytochrome negatively autoregulates the torCAD operon probably by inhibiting the TorS kinase activity.

Subunit structure

The N-terminal domain interacts with TorA. The immature C-terminal domain can bind to the N-terminal detector region of TorS.

Subcellular location

Cell inner membrane; Single-pass type II membrane protein.

Post-translational modification

Binds 5 heme groups per subunit By similarity.

Sequence similarities

Belongs to the TorC/TorY family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 390390Cytochrome c-type protein TorC
PRO_0000108427

Regions

Topological domain1 – 1616Cytoplasmic Potential
Transmembrane17 – 3721Helical; Potential
Topological domain38 – 390353Periplasmic Potential

Sites

Metal binding521Iron (heme 1 axial ligand) By similarity
Metal binding811Iron (heme 2 axial ligand) By similarity
Metal binding1421Iron (heme 3 axial ligand) By similarity
Metal binding1741Iron (heme 4 axial ligand) By similarity
Metal binding3331Iron (heme 5 axial ligand) By similarity
Binding site481Heme 1 (covalent) By similarity
Binding site511Heme 1 (covalent) By similarity
Binding site771Heme 2 (covalent) By similarity
Binding site801Heme 2 (covalent) By similarity
Binding site1381Heme 3 (covalent) By similarity
Binding site1411Heme 3 (covalent) By similarity
Binding site1701Heme 4 (covalent) By similarity
Binding site1731Heme 4 (covalent) By similarity
Binding site3291Heme 5 (covalent) By similarity
Binding site3321Heme 5 (covalent) By similarity

Experimental info

Mutagenesis3291C → S: Decrease in expression of the torCAD operon. Ref.9
Sequence conflict194 – 1952EL → DV in CAA52094. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P33226 [UniParc].

Last modified November 1, 1997. Version 3.
Checksum: 3035F71D4B32F22B

FASTA39043,607
        10         20         30         40         50         60 
MRKLWNALRR PSARWSVLAL VAIGIVIGIA LIVLPHVGIK VTSTTEFCVS CHSMQPVYEE 

        70         80         90        100        110        120 
YKQSVHFQNA SGVRAECHDC HIPPDIPGMV KRKLEASNDI YQTFIAHSID TPEKFEAKRA 

       130        140        150        160        170        180 
ELAEREWARM KENNSATCRS CHNYDAMDHA KQHPEAARQM KVAAKDNQSC IDCHKGIAHQ 

       190        200        210        220        230        240 
LPDMSSGFRK QFDELRASAN DSGDTLYSID IKPIYAAKGD KEASGSLLPA SEVKVLKRDG 

       250        260        270        280        290        300 
DWLQIEITGW TESAGRQRVL TQFPGKRIFV ASIRGDVQQQ VKTLEKTTVA DTNTEWSKLQ 

       310        320        330        340        350        360 
ATAWMKKGDM VNDIKPIWAY ADSLYNGTCN QCHGAPEIAH FDANGWIGTL NGMIGFTSLD 

       370        380        390 
KREERTLLKY LQMNASDTAG KAHGDKKEEK 

« Hide

References

« Hide 'large scale' references
[1]"TMAO anaerobic respiration in Escherichia coli: involvement of the tor operon."
Mejean V., Iobbi-Nivol C., Lepelletier M., Giordano G., Chippaux M., Pascal M.-C.
Mol. Microbiol. 11:1169-1179(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]Pascal M.-C.
Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 73-76.
[3]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"A reassessment of the range of c-type cytochromes synthesized by Escherichia coli K-12."
Iobbi-Nivol C., Crooke H., Griffiths L., Grov J., Hussain H., Pommier J., Mejean V., Cole J.A.
FEMS Microbiol. Lett. 119:89-94(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION AS A CYTOCHROME C.
[7]"TorC apocytochrome negatively autoregulates the trimethylamine N-oxide (TMAO) reductase operon in Escherichia coli."
Ansaldi M., Bordi C., Lepelletier M., Mejean V.
Mol. Microbiol. 33:284-295(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[8]"Electron transfer and binding of the c-type cytochrome TorC to the trimethylamine N-oxide reductase in Escherichia coli."
Gon S., Giudici-Orticoni M.-T., Mejean V., Iobbi-Nivol C.
J. Biol. Chem. 276:11545-11551(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[9]"An unsuspected autoregulatory pathway involving apocytochrome TorC and sensor TorS in Escherichia coli."
Gon S., Jourlin-Castelli C., Theraulaz L., Mejean V.
Proc. Natl. Acad. Sci. U.S.A. 98:11615-11620(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, MUTAGENESIS OF CYS-329.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X73888 Genomic DNA. Translation: CAA52094.1.
U00096 Genomic DNA. Translation: AAC74081.1.
AP009048 Genomic DNA. Translation: BAA36138.1.
PIRS34221. B64841.
RefSeqNP_415516.1. NC_000913.3.
YP_489269.1. NC_007779.1.

3D structure databases

ProteinModelPortalP33226.
SMRP33226. Positions 20-179, 323-380.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-11014N.
IntActP33226. 1 interaction.
MINTMINT-1285841.
STRING511145.b0996.

Protein family/group databases

TCDB5.A.3.4.1. the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.

Proteomic databases

PRIDEP33226.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74081; AAC74081; b0996.
BAA36138; BAA36138; BAA36138.
GeneID12932501.
946252.
KEGGecj:Y75_p0969.
eco:b0996.
PATRIC32117217. VBIEscCol129921_1032.

Organism-specific databases

EchoBASEEB1762.
EcoGeneEG11815. torC.

Phylogenomic databases

eggNOGCOG3005.
HOGENOMHOG000284378.
KOK03532.
OMADSATCRT.
OrthoDBEOG6RNQDS.
ProtClustDBPRK15032.

Enzyme and pathway databases

BioCycEcoCyc:EG11815-MONOMER.
ECOL316407:JW0981-MONOMER.
MetaCyc:EG11815-MONOMER.

Gene expression databases

GenevestigatorP33226.

Family and domain databases

InterProIPR009154. Membr-bd_4haem_cyt_TorC.
IPR011031. Multihaem_cyt.
IPR005126. NapC/NirT_cyt_c_N.
[Graphical view]
PfamPF03264. Cytochrom_NNT. 1 hit.
[Graphical view]
PIRSFPIRSF000014. 4_hem_cytch_TorC. 1 hit.
TIGRFAMsTIGR02162. torC. 1 hit.
PROSITEPS51008. MULTIHEME_CYTC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP33226.

Entry information

Entry nameTORC_ECOLI
AccessionPrimary (citable) accession number: P33226
Secondary accession number(s): P77446
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: November 1, 1997
Last modified: March 19, 2014
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene