TORC_ECOLI
ID TORC_ECOLI Reviewed; 390 AA.
AC P33226; P77446;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Cytochrome c-type protein TorC;
GN Name=torC; OrderedLocusNames=b0996, JW0981;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8022286; DOI=10.1111/j.1365-2958.1994.tb00393.x;
RA Mejean V., Iobbi-Nivol C., Lepelletier M., Giordano G., Chippaux M.,
RA Pascal M.-C.;
RT "TMAO anaerobic respiration in Escherichia coli: involvement of the tor
RT operon.";
RL Mol. Microbiol. 11:1169-1179(1994).
RN [2]
RP SEQUENCE REVISION TO 73-76.
RA Pascal M.-C.;
RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP CHARACTERIZATION AS A CYTOCHROME C.
RX PubMed=8039676; DOI=10.1111/j.1574-6968.1994.tb06872.x;
RA Iobbi-Nivol C., Crooke H., Griffiths L., Grov J., Hussain H., Pommier J.,
RA Mejean V., Cole J.A.;
RT "A reassessment of the range of c-type cytochromes synthesized by
RT Escherichia coli K-12.";
RL FEMS Microbiol. Lett. 119:89-94(1994).
RN [7]
RP CHARACTERIZATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=10411745; DOI=10.1046/j.1365-2958.1999.01468.x;
RA Ansaldi M., Bordi C., Lepelletier M., Mejean V.;
RT "TorC apocytochrome negatively autoregulates the trimethylamine N-oxide
RT (TMAO) reductase operon in Escherichia coli.";
RL Mol. Microbiol. 33:284-295(1999).
RN [8]
RP CHARACTERIZATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11056172; DOI=10.1074/jbc.m008875200;
RA Gon S., Giudici-Orticoni M.-T., Mejean V., Iobbi-Nivol C.;
RT "Electron transfer and binding of the c-type cytochrome TorC to the
RT trimethylamine N-oxide reductase in Escherichia coli.";
RL J. Biol. Chem. 276:11545-11551(2001).
RN [9]
RP CHARACTERIZATION, AND MUTAGENESIS OF CYS-329.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11562502; DOI=10.1073/pnas.211330598;
RA Gon S., Jourlin-Castelli C., Theraulaz L., Mejean V.;
RT "An unsuspected autoregulatory pathway involving apocytochrome TorC and
RT sensor TorS in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:11615-11620(2001).
CC -!- FUNCTION: Part of the anaerobic respiratory chain of trimethylamine-N-
CC oxide reductase TorA. Acts by transferring electrons from the
CC membranous menaquinones to TorA. This transfer probably involves an
CC electron transfer pathway from menaquinones to the N-terminal domain of
CC TorC, then from the N-terminus to the C-terminus, and finally to TorA.
CC TorC apocytochrome negatively autoregulates the torCAD operon probably
CC by inhibiting the TorS kinase activity.
CC -!- SUBUNIT: The N-terminal domain interacts with TorA. The immature C-
CC terminal domain can bind to the N-terminal detector region of TorS.
CC -!- INTERACTION:
CC P33226; P33225: torA; NbExp=3; IntAct=EBI-553710, EBI-557008;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane
CC protein.
CC -!- PTM: Binds 5 heme groups per subunit. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TorC/TorY family. {ECO:0000305}.
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DR EMBL; X73888; CAA52094.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74081.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36138.1; -; Genomic_DNA.
DR PIR; B64841; S34221.
DR RefSeq; NP_415516.1; NC_000913.3.
DR RefSeq; WP_001230242.1; NZ_SSZK01000002.1.
DR AlphaFoldDB; P33226; -.
DR BioGRID; 4261495; 10.
DR ComplexPortal; CPX-319; Trimethylamine-N-oxide reductase TorAC complex.
DR DIP; DIP-11014N; -.
DR IntAct; P33226; 2.
DR STRING; 511145.b0996; -.
DR TCDB; 5.A.3.4.1; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR PaxDb; P33226; -.
DR PRIDE; P33226; -.
DR EnsemblBacteria; AAC74081; AAC74081; b0996.
DR EnsemblBacteria; BAA36138; BAA36138; BAA36138.
DR GeneID; 66670726; -.
DR GeneID; 946252; -.
DR KEGG; ecj:JW0981; -.
DR KEGG; eco:b0996; -.
DR PATRIC; fig|1411691.4.peg.1275; -.
DR EchoBASE; EB1762; -.
DR eggNOG; COG3005; Bacteria.
DR HOGENOM; CLU_058814_0_0_6; -.
DR OMA; MISRIWK; -.
DR PhylomeDB; P33226; -.
DR BioCyc; EcoCyc:EG11815-MON; -.
DR BioCyc; MetaCyc:EG11815-MON; -.
DR PRO; PR:P33226; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; ISM:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1904852; C:trimethylamine-N-oxide reductase (cytochrome c) complex; IPI:ComplexPortal.
DR GO; GO:0009055; F:electron transfer activity; IDA:EcoCyc.
DR GO; GO:0020037; F:heme binding; IDA:EcoCyc.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0009060; P:aerobic respiration; IDA:ComplexPortal.
DR GO; GO:0019645; P:anaerobic electron transport chain; IDA:ComplexPortal.
DR GO; GO:0009061; P:anaerobic respiration; IEP:EcoCyc.
DR GO; GO:0009968; P:negative regulation of signal transduction; IDA:EcoCyc.
DR GO; GO:0006885; P:regulation of pH; IDA:ComplexPortal.
DR Gene3D; 1.10.3820.10; -; 1.
DR InterPro; IPR009154; Membr-bd_4haem_cyt_TorC.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR InterPro; IPR005126; NapC/NirT_cyt_c_N.
DR InterPro; IPR038266; NapC/NirT_cytc_sf.
DR Pfam; PF03264; Cytochrom_NNT; 1.
DR PIRSF; PIRSF000014; 4_hem_cytch_TorC; 1.
DR SUPFAM; SSF48695; SSF48695; 1.
DR TIGRFAMs; TIGR02162; torC; 1.
DR PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..390
FT /note="Cytochrome c-type protein TorC"
FT /id="PRO_0000108427"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..390
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT BINDING 48
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 332
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 333
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="5"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT MUTAGEN 329
FT /note="C->S: Decrease in expression of the torCAD operon."
FT /evidence="ECO:0000269|PubMed:11562502"
FT CONFLICT 194..195
FT /note="EL -> DV (in Ref. 1; CAA52094)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 390 AA; 43607 MW; 3035F71D4B32F22B CRC64;
MRKLWNALRR PSARWSVLAL VAIGIVIGIA LIVLPHVGIK VTSTTEFCVS CHSMQPVYEE
YKQSVHFQNA SGVRAECHDC HIPPDIPGMV KRKLEASNDI YQTFIAHSID TPEKFEAKRA
ELAEREWARM KENNSATCRS CHNYDAMDHA KQHPEAARQM KVAAKDNQSC IDCHKGIAHQ
LPDMSSGFRK QFDELRASAN DSGDTLYSID IKPIYAAKGD KEASGSLLPA SEVKVLKRDG
DWLQIEITGW TESAGRQRVL TQFPGKRIFV ASIRGDVQQQ VKTLEKTTVA DTNTEWSKLQ
ATAWMKKGDM VNDIKPIWAY ADSLYNGTCN QCHGAPEIAH FDANGWIGTL NGMIGFTSLD
KREERTLLKY LQMNASDTAG KAHGDKKEEK
