TORY_ECOLI
ID TORY_ECOLI Reviewed; 366 AA.
AC P52005; P76293;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Cytochrome c-type protein TorY;
GN Name=torY; Synonyms=yecK; OrderedLocusNames=b1873, JW1862;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 292-366.
RC STRAIN=K12 / ACC5;
RX PubMed=8919859; DOI=10.1007/bf02198832;
RA del Campillo-Campbell A., Campbell A.M.;
RT "Alternative gene for biotin sulfoxide reduction in Escherichia coli K-
RT 12.";
RL J. Mol. Evol. 42:85-90(1996).
RN [5]
RP IDENTIFICATION.
RA Rudd K.E.;
RL Unpublished observations (MAR-1996).
RN [6]
RP CHARACTERIZATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11004177; DOI=10.1128/jb.182.20.5779-5786.2000;
RA Gon S., Patte J.-C., Mejean V., Iobbi-Nivol C.;
RT "The torYZ (yecK bisZ) operon encodes a third respiratory trimethylamine N-
RT oxide reductase in Escherichia coli.";
RL J. Bacteriol. 182:5779-5786(2000).
CC -!- FUNCTION: Part of the anaerobic respiratory chain of trimethylamine-N-
CC oxide reductase TorZ. Required for electron transfer to the TorZ
CC terminal enzyme.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-pass
CC type II membrane protein {ECO:0000250}.
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; U00096; AAC74943.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15683.1; -; Genomic_DNA.
DR EMBL; U38839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A64950; A64950.
DR RefSeq; NP_416387.1; NC_000913.3.
DR RefSeq; WP_001214331.1; NZ_LN832404.1.
DR AlphaFoldDB; P52005; -.
DR BioGRID; 4260350; 13.
DR DIP; DIP-11829N; -.
DR IntAct; P52005; 2.
DR STRING; 511145.b1873; -.
DR TCDB; 5.A.3.4.2; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR PaxDb; P52005; -.
DR PRIDE; P52005; -.
DR EnsemblBacteria; AAC74943; AAC74943; b1873.
DR EnsemblBacteria; BAA15683; BAA15683; BAA15683.
DR GeneID; 946490; -.
DR KEGG; ecj:JW1862; -.
DR KEGG; eco:b1873; -.
DR PATRIC; fig|1411691.4.peg.375; -.
DR EchoBASE; EB3062; -.
DR eggNOG; COG3005; Bacteria.
DR HOGENOM; CLU_058814_0_0_6; -.
DR OMA; FNANQWI; -.
DR PhylomeDB; P52005; -.
DR BioCyc; EcoCyc:G7023-MON; -.
DR PRO; PR:P52005; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:InterPro.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR GO; GO:0009055; F:electron transfer activity; IMP:EcoCyc.
DR GO; GO:0020037; F:heme binding; ISM:EcoCyc.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0019645; P:anaerobic electron transport chain; IMP:EcoCyc.
DR GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
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 PROSITE; PS51008; MULTIHEME_CYTC; 2.
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..366
FT /note="Cytochrome c-type protein TorY"
FT /id="PRO_0000108429"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..366
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT BINDING 39
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 42
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 43
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 68
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 71
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 72
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 129
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 133
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 161
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 165
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 313
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 317
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"
SQ SEQUENCE 366 AA; 40286 MW; 1ED252C9882D98E3 CRC64;
MRGKKRIGLL FLLIAVVVGG GGLLLAQKVL HKTSDTAFCL SCHSMSKPFE EYQGTVHFSN
QKGIRAECAD CHIPKSGMDY LFAKLKASKD IYHEFVSGKI DSDDKFEAHR QEMAETVWKE
LKATDSATCR SCHSFDAMDI ASQSESAQKM HNKAQKDSET CIDCHKGIAH FPPEIKMDDN
AAHELESQAA TSVTNGAHIY PFKTSHIGEL ATVNPGTDLT VVDASGKQPI VLLQGYQMQG
SENTLYLAAG QRLALATLSE EGIKALTVNG EWQADEYGNQ WRQASLQGAL TDPALADRKP
LWQYAEKLDD TYCAGCHAPI AADHYTVNAW PSIAKGMGAR TSMSENELDI LTRYFQYNAK
DITEKQ
