YDHU_ECOLI
ID YDHU_ECOLI Reviewed; 261 AA.
AC P77409;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Putative cytochrome YdhU {ECO:0000305};
DE AltName: Full=Protein PhsC homolog {ECO:0000305};
GN Name=ydhU; OrderedLocusNames=b1670, JW1660;
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 / MG1655 / ATCC 47076;
RX PubMed=9023191; DOI=10.1128/jb.179.4.1105-1111.1997;
RA Hensel M., Shea J.E., Baeumler A.J., Gleeson C., Blattner F.R.,
RA Holden D.W.;
RT "Analysis of the boundaries of Salmonella pathogenicity island 2 and the
RT corresponding chromosomal region of Escherichia coli K-12.";
RL J. Bacteriol. 179:1105-1111(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [3]
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 [4]
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 [5]
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=18227264; DOI=10.1099/mic.0.2007/012146-0;
RA Partridge J.D., Browning D.F., Xu M., Newnham L.J., Scott C., Roberts R.E.,
RA Poole R.K., Green J.;
RT "Characterization of the Escherichia coli K-12 ydhYVWXUT operon: regulation
RT by FNR, NarL and NarP.";
RL Microbiology 154:608-618(2008).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P0AEK7};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- INDUCTION: Up-regulated by the oxygen-responsive transcription factor
CC FNR under anaerobic conditions. Repressed in the presence of nitrate or
CC nitrite via the two-component systems NarXL and NarPQ, respectively.
CC {ECO:0000269|PubMed:18227264}.
CC -!- SIMILARITY: Belongs to the PhsC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U68703; AAB47946.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74740.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15442.1; -; Genomic_DNA.
DR PIR; F64924; F64924.
DR RefSeq; NP_416185.1; NC_000913.3.
DR RefSeq; WP_001069979.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P77409; -.
DR SMR; P77409; -.
DR BioGRID; 4262230; 6.
DR BioGRID; 849981; 1.
DR DIP; DIP-11740N; -.
DR IntAct; P77409; 4.
DR STRING; 511145.b1670; -.
DR PaxDb; P77409; -.
DR PRIDE; P77409; -.
DR EnsemblBacteria; AAC74740; AAC74740; b1670.
DR EnsemblBacteria; BAA15442; BAA15442; BAA15442.
DR GeneID; 945608; -.
DR KEGG; ecj:JW1660; -.
DR KEGG; eco:b1670; -.
DR PATRIC; fig|1411691.4.peg.589; -.
DR EchoBASE; EB3713; -.
DR eggNOG; COG4117; Bacteria.
DR HOGENOM; CLU_097472_0_0_6; -.
DR InParanoid; P77409; -.
DR OMA; ITGWEEV; -.
DR PhylomeDB; P77409; -.
DR BioCyc; EcoCyc:G6898-MON; -.
DR PRO; PR:P77409; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR InterPro; IPR011577; Cyt_b561_bac/Ni-Hgenase.
DR InterPro; IPR016174; Di-haem_cyt_TM.
DR Pfam; PF01292; Ni_hydr_CYTB; 1.
DR SUPFAM; SSF81342; SSF81342; 1.
PE 2: Evidence at transcript level;
KW Cell inner membrane; Cell membrane; Iron; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..261
FT /note="Putative cytochrome YdhU"
FT /id="PRO_0000058407"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 77
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P0AEK7"
FT BINDING 111
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P0AEK7"
FT BINDING 223
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P0AEK7"
FT BINDING 237
FT /ligand="a menaquinone"
FT /ligand_id="ChEBI:CHEBI:16374"
FT /evidence="ECO:0000250|UniProtKB:P0AEK7"
FT BINDING 237
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P0AEK7"
SQ SEQUENCE 261 AA; 29583 MW; 65CF1A45691A0AF3 CRC64;
MNPSQHAEQF QSQLANYVPQ FTPEFWPVWL IIAGVLLVGM WLVLGLHALL RARGVKKSAT
DHGEKIYLYS KAVRLWHWSN ALLFVLLLAS GLINHFAMVG ATAVKSLVAV HEVCGFLLLA
CWLGFVLINA VGDNGHHYRI RRQGWLERAA KQTRFYLFGI MQGEEHPFPA TTQSKFNPLQ
QVAYVGVMYG LLPLLLLTGL LCLYPQAVGD VFPGVRYWLL QTHFALAFIS LFFIFGHLYL
CTTGRTPHET FKSMVDGYHR H