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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}.
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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
 
 
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