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Database: UniProt
Entry: D7DKM2_METV0
LinkDB: D7DKM2_METV0
Original site: D7DKM2_METV0 
ID   D7DKM2_METV0            Unreviewed;       202 AA.
AC   D7DKM2;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=Ubiquinone biosynthesis accessory factor UbiJ {ECO:0000256|HAMAP-Rule:MF_02215};
GN   Name=ubiJ {ECO:0000256|HAMAP-Rule:MF_02215};
GN   OrderedLocusNames=M301_2099 {ECO:0000313|EMBL:ADI30468.1};
OS   Methylotenera versatilis (strain 301).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylotenera.
OX   NCBI_TaxID=666681 {ECO:0000313|EMBL:ADI30468.1, ECO:0000313|Proteomes:UP000000383};
RN   [1] {ECO:0000313|Proteomes:UP000000383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 {ECO:0000313|Proteomes:UP000000383};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Clum A., Land M., Hauser L., Kyrpides N., Ivanova N.,
RA   Chistoservova L., Kalyuzhnaya M., Woyke T.;
RT   "Complete sequence of Methylotenera sp. 301.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADI30468.1, ECO:0000313|Proteomes:UP000000383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 {ECO:0000313|EMBL:ADI30468.1,
RC   ECO:0000313|Proteomes:UP000000383};
RX   PubMed=21622745; DOI=10.1128/JB.00404-11;
RA   Lapidus A., Clum A., Labutti K., Kaluzhnaya M.G., Lim S., Beck D.A.,
RA   Glavina Del Rio T., Nolan M., Mavromatis K., Huntemann M., Lucas S.,
RA   Lidstrom M.E., Ivanova N., Chistoserdova L.;
RT   "Genomes of three methylotrophs from a single niche uncover genetic and
RT   metabolic divergence of Methylophilaceae.";
RL   J. Bacteriol. 193:3757-3764(2011).
CC   -!- FUNCTION: Required for ubiquinone (coenzyme Q) biosynthesis. Binds
CC       hydrophobic ubiquinone biosynthetic intermediates via its SCP2 domain
CC       and is essential for the stability of the Ubi complex. May constitute a
CC       docking platform where Ubi enzymes assemble and access their SCP2-bound
CC       polyprenyl substrates. {ECO:0000256|HAMAP-Rule:MF_02215}.
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_02215}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02215}.
CC   -!- SIMILARITY: Belongs to the UbiJ family. {ECO:0000256|HAMAP-
CC       Rule:MF_02215}.
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DR   EMBL; CP002056; ADI30468.1; -; Genomic_DNA.
DR   RefSeq; WP_013148777.1; NC_014207.1.
DR   AlphaFoldDB; D7DKM2; -.
DR   STRING; 666681.M301_2099; -.
DR   KEGG; meh:M301_2099; -.
DR   eggNOG; COG3165; Bacteria.
DR   HOGENOM; CLU_100130_0_0_4; -.
DR   OrthoDB; 8525483at2; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000000383; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0032150; P:ubiquinone biosynthetic process from chorismate; IEA:InterPro.
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:SF1; UBIQUINONE BIOSYNTHESIS ACCESSORY FACTOR UBIJ; 1.
DR   PANTHER; PTHR38693; UBIQUINONE BIOSYNTHESIS PROTEIN UBIJ; 1.
DR   Pfam; PF02036; SCP2; 1.
DR   SUPFAM; SSF55718; SCP-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02215};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000383};
KW   Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_02215}.
FT   DOMAIN          10..101
FT                   /note="SCP2"
FT                   /evidence="ECO:0000259|Pfam:PF02036"
SQ   SEQUENCE   202 AA;  22375 MW;  E2BEB4D8C0E425EE CRC64;
     MLKALSTRLL QHLISQNSWA SNLLKPFAGR SIQINVSFIS ASLVILENGN LAMAGETNVP
     DAKVTIPPSL LLRLLAKDET ANRQINIEGD TQLVAELAKV FSNMRWDYED DLSSLIGDIP
     ANKIGTFARD AANSVKETSI NLAEMLSEYW QEEMPLIAKK RHVEQFNAEV DILGADVARF
     EKRLAKLTKS IKANLDNGLL KN
//
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