UBIJ_ECOLI
ID UBIJ_ECOLI Reviewed; 201 AA.
AC P0ADP7; P27852; Q2M8D9;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Ubiquinone biosynthesis accessory factor UbiJ {ECO:0000255|HAMAP-Rule:MF_02215, ECO:0000305};
GN Name=ubiJ {ECO:0000255|HAMAP-Rule:MF_02215, ECO:0000303|PubMed:24142253};
GN Synonyms=yigP; OrderedLocusNames=b3834, JW3811;
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 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 119-139.
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 FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=24142253; DOI=10.1128/jb.01065-13;
RA Aussel L., Loiseau L., Hajj Chehade M., Pocachard B., Fontecave M.,
RA Pierrel F., Barras F.;
RT "ubiJ, a new gene required for aerobic growth and proliferation in
RT macrophage, is involved in coenzyme Q biosynthesis in Escherichia coli and
RT Salmonella enterica serovar Typhimurium.";
RL J. Bacteriol. 196:70-79(2014).
RN [5]
RP INTERACTION WITH UBIK.
RX PubMed=28559279; DOI=10.1074/jbc.m117.789164;
RA Loiseau L., Fyfe C., Aussel L., Hajj Chehade M., Hernandez S.B., Faivre B.,
RA Hamdane D., Mellot-Draznieks C., Rascalou B., Pelosi L., Velours C.,
RA Cornu D., Lombard M., Casadesus J., Pierrel F., Fontecave M., Barras F.;
RT "The UbiK protein is an accessory factor necessary for bacterial ubiquinone
RT (UQ) biosynthesis and forms a complex with the UQ biogenesis factor UbiJ.";
RL J. Biol. Chem. 292:11937-11950(2017).
RN [6] {ECO:0007744|PDB:6H6N, ECO:0007744|PDB:6H6O, ECO:0007744|PDB:6H6P}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-120, FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=30686758; DOI=10.1016/j.chembiol.2018.12.001;
RA Hajj Chehade M., Pelosi L., Fyfe C.D., Loiseau L., Rascalou B.,
RA Brugiere S., Kazemzadeh K., Vo C.D., Ciccone L., Aussel L., Coute Y.,
RA Fontecave M., Barras F., Lombard M., Pierrel F.;
RT "A soluble metabolon synthesizes the isoprenoid lipid ubiquinone.";
RL Cell Chem. Biol. 26:482-492(2019).
CC -!- FUNCTION: Required for ubiquinone (coenzyme Q) biosynthesis under
CC aerobic conditions (PubMed:24142253, PubMed:30686758). Binds
CC hydrophobic ubiquinone biosynthetic intermediates via its SCP2 domain
CC and is essential for the stability of the Ubi complex
CC (PubMed:30686758). May constitute a docking platform where Ubi enzymes
CC assemble and access their SCP2-bound polyprenyl substrates
CC (PubMed:30686758). {ECO:0000269|PubMed:24142253,
CC ECO:0000269|PubMed:30686758}.
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02215, ECO:0000269|PubMed:24142253}.
CC -!- SUBUNIT: Component of the Ubi complex metabolon, which regroups five
CC ubiquinone biosynthesis proteins (UbiE, UbiF, UbiG, UbiH and UbiI) and
CC two accessory factors (UbiK and the lipid-binding protein UbiJ)
CC (PubMed:30686758). Interacts with UbiK and forms a complex composed of
CC 2 UbiK subunits and 1 UbiJ subunit. The UbiK-UbiJ complex interacts
CC with palmitoleic acid (PubMed:28559279). {ECO:0000269|PubMed:28559279,
CC ECO:0000269|PubMed:30686758}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02215,
CC ECO:0000269|PubMed:30686758}.
CC -!- DISRUPTION PHENOTYPE: During aerobic growth, mutant is impaired for
CC ubiquinone biosynthesis and for growth in rich medium, but it does not
CC present any defect under anaerobic conditions.
CC {ECO:0000269|PubMed:24142253}.
CC -!- SIMILARITY: Belongs to the UbiJ family. {ECO:0000255|HAMAP-
CC Rule:MF_02215, ECO:0000305}.
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DR EMBL; M87049; AAA67629.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76837.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77467.1; -; Genomic_DNA.
DR PIR; C65188; C65188.
DR RefSeq; NP_418278.1; NC_000913.3.
DR RefSeq; WP_001295259.1; NZ_STEB01000021.1.
DR PDB; 6H6N; X-ray; 2.12 A; A/B=1-120.
DR PDB; 6H6O; X-ray; 1.70 A; A/B=1-120.
DR PDB; 6H6P; X-ray; 2.50 A; A/B/C/D=1-120.
DR PDBsum; 6H6N; -.
DR PDBsum; 6H6O; -.
DR PDBsum; 6H6P; -.
DR AlphaFoldDB; P0ADP7; -.
DR SMR; P0ADP7; -.
DR BioGRID; 4260947; 1.
DR IntAct; P0ADP7; 1.
DR STRING; 511145.b3834; -.
DR jPOST; P0ADP7; -.
DR PaxDb; P0ADP7; -.
DR PRIDE; P0ADP7; -.
DR EnsemblBacteria; AAC76837; AAC76837; b3834.
DR EnsemblBacteria; BAE77467; BAE77467; BAE77467.
DR GeneID; 66672258; -.
DR GeneID; 948915; -.
DR KEGG; ecj:JW3811; -.
DR KEGG; eco:b3834; -.
DR PATRIC; fig|511145.12.peg.3950; -.
DR EchoBASE; EB1442; -.
DR eggNOG; COG3165; Bacteria.
DR HOGENOM; CLU_100130_2_0_6; -.
DR OMA; LELDWEY; -.
DR PhylomeDB; P0ADP7; -.
DR BioCyc; EcoCyc:EG11474-MON; -.
DR BioCyc; MetaCyc:EG11474-MON; -.
DR UniPathway; UPA00232; -.
DR PRO; PR:P0ADP7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0110142; C:ubiquinone biosynthesis complex; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IMP:EcoCyc.
DR GO; GO:0032150; P:ubiquinone biosynthetic process from chorismate; IMP:EcoCyc.
DR HAMAP; MF_02215; UbiJ; 1.
DR InterPro; IPR003033; SCP2_sterol-bd_dom.
DR InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
DR InterPro; IPR038989; UbiJ.
DR PANTHER; PTHR38693; PTHR38693; 1.
DR Pfam; PF02036; SCP2; 1.
DR SUPFAM; SSF55718; SSF55718; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Ubiquinone biosynthesis.
FT CHAIN 1..201
FT /note="Ubiquinone biosynthesis accessory factor UbiJ"
FT /id="PRO_0000169668"
FT DOMAIN 15..112
FT /note="SCP2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02215"
FT CONFLICT 119..139
FT /note="PAELLAPYTGDIAAEGISKAM -> LRNCWPLIPVISPLKESAKP (in
FT Ref. 1; AAA67629)"
FT /evidence="ECO:0000305"
FT HELIX 3..19
FT /evidence="ECO:0007829|PDB:6H6O"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:6H6O"
FT HELIX 26..30
FT /evidence="ECO:0007829|PDB:6H6O"
FT TURN 31..34
FT /evidence="ECO:0007829|PDB:6H6O"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:6H6O"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:6H6O"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:6H6O"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:6H6O"
FT HELIX 75..80
FT /evidence="ECO:0007829|PDB:6H6O"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:6H6O"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:6H6O"
FT HELIX 102..117
FT /evidence="ECO:0007829|PDB:6H6O"
SQ SEQUENCE 201 AA; 22153 MW; 9C64980A59992A2E CRC64;
MPFKPLVTAG IESLLNTFLY RSPALKTARS RLLGKVLRVE VKGFSTSLIL VFSERQVDVL
GEWAGDADCT VIAYASVLPK LRDRQQLTAL IRSGELEVQG DIQVVQNFVA LADLAEFDPA
ELLAPYTGDI AAEGISKAMR GGAKFLHHGI KRQQRYVAEA ITEEWRMAPG PLEVAWFAEE
TAAVERAVDA LTKRLEKLEA K
