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Database: UniProt
Entry: U3CQW3_9VIBR
LinkDB: U3CQW3_9VIBR
Original site: U3CQW3_9VIBR 
ID   U3CQW3_9VIBR            Unreviewed;       201 AA.
AC   U3CQW3;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Ubiquinone biosynthesis accessory factor UbiJ {ECO:0000256|HAMAP-Rule:MF_02215};
GN   Name=ubiJ {ECO:0000256|HAMAP-Rule:MF_02215};
GN   ORFNames=VEZ01S_37_00480 {ECO:0000313|EMBL:GAD80483.1};
OS   Vibrio ezurae NBRC 102218.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1219080 {ECO:0000313|EMBL:GAD80483.1, ECO:0000313|Proteomes:UP000016562};
RN   [1] {ECO:0000313|EMBL:GAD80483.1, ECO:0000313|Proteomes:UP000016562}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 102218 {ECO:0000313|EMBL:GAD80483.1,
RC   ECO:0000313|Proteomes:UP000016562};
RA   Yoshida I., Hosoyama A., Numata M., Hashimoto M., Hosoyama Y.,
RA   Tsuchikane K., Noguchi M., Hirakata S., Ichikawa N., Ohji S., Yamazoe A.,
RA   Fujita N.;
RT   "Whole genome shotgun sequence of Vibrio ezurae NBRC 102218.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAD80483.1}.
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DR   EMBL; BATM01000037; GAD80483.1; -; Genomic_DNA.
DR   RefSeq; WP_021714191.1; NZ_BATM01000037.1.
DR   AlphaFoldDB; U3CQW3; -.
DR   STRING; 1219080.VEZ01S_37_00480; -.
DR   eggNOG; COG3165; Bacteria.
DR   OrthoDB; 5801225at2; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000016562; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0032150; P:ubiquinone biosynthetic process from chorismate; IEA:InterPro.
DR   Gene3D; 3.30.1050.10; SCP2 sterol-binding domain; 1.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02215};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016562};
KW   Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_02215}.
FT   DOMAIN          15..112
FT                   /note="SCP2"
FT                   /evidence="ECO:0000259|Pfam:PF02036"
FT   COILED          173..200
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   201 AA;  22043 MW;  6329DAE0DAF19053 CRC64;
     MPIDSLVTAA VEVSFNSLIK QQPESQKQLA RMKGSTIRLN LKELNKSLIF VCSQQIDVLA
     SFEGTPDCEL TLSLTALRDL QQQANINELF KQDKLSVAGD MQVGQQFATL MQLSKPDIAE
     ILSKVVGDVA AHTLVSGAKN GLSFLQNSAQ KHTSHLKHVV TEEWQLAPSP LAVANFCDQV
     DDVQAKLASL EQRLSRLTET E
//
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