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Database: UniProt
Entry: A0A2J8GV96_VIBDI
LinkDB: A0A2J8GV96_VIBDI
Original site: A0A2J8GV96_VIBDI 
ID   A0A2J8GV96_VIBDI        Unreviewed;       292 AA.
AC   A0A2J8GV96;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Ubiquinone biosynthesis protein UbiV {ECO:0000256|HAMAP-Rule:MF_02233};
GN   Name=ubiV {ECO:0000256|HAMAP-Rule:MF_02233};
GN   ORFNames=C1N32_09485 {ECO:0000313|EMBL:PNI05020.1}, DET48_102131
GN   {ECO:0000313|EMBL:RAS69302.1};
OS   Vibrio diazotrophicus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=685 {ECO:0000313|EMBL:RAS69302.1, ECO:0000313|Proteomes:UP000248729};
RN   [1] {ECO:0000313|EMBL:PNI05020.1, ECO:0000313|Proteomes:UP000236449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=60.27F {ECO:0000313|EMBL:PNI05020.1,
RC   ECO:0000313|Proteomes:UP000236449};
RA   Castillo D., Vandieken V., Chiang O., Middelboe M.;
RT   "Draft genome sequences of six Vibrio diazotrophicus strains isolated from
RT   deep-sea sediments of the Baltic Sea.";
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RAS69302.1, ECO:0000313|Proteomes:UP000248729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=99A {ECO:0000313|EMBL:RAS69302.1,
RC   ECO:0000313|Proteomes:UP000248729};
RA   Lamendella R.;
RT   "Freshwater and sediment microbial communities from various areas in North
RT   America, analyzing microbe dynamics in response to fracking.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for O(2)-independent ubiquinone (coenzyme Q)
CC       biosynthesis. Together with UbiU, is essential for the C6-hydroxylation
CC       reaction in the oxygen-independent ubiquinone biosynthesis pathway.
CC       {ECO:0000256|HAMAP-Rule:MF_02233}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02233};
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_02233}.
CC   -!- SUBUNIT: Forms an heterodimer with UbiU. {ECO:0000256|HAMAP-
CC       Rule:MF_02233}.
CC   -!- SIMILARITY: Belongs to the peptidase U32 family. UbiV subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_02233}.
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:RAS69302.1}.
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DR   EMBL; POSK01000005; PNI05020.1; -; Genomic_DNA.
DR   EMBL; QLTR01000002; RAS69302.1; -; Genomic_DNA.
DR   STRING; 1348635.GCA_000740015_03770; -.
DR   OrthoDB; 8523349at2; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000236449; Unassembled WGS sequence.
DR   Proteomes; UP000248729; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_02233; UbiV; 1.
DR   InterPro; IPR001539; Peptidase_U32.
DR   InterPro; IPR043693; UbiV.
DR   PANTHER; PTHR30217; PEPTIDASE U32 FAMILY; 1.
DR   PANTHER; PTHR30217:SF11; UBIQUINONE BIOSYNTHESIS PROTEIN UBIV; 1.
DR   Pfam; PF01136; Peptidase_U32; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_02233};
KW   Hydrolase {ECO:0000313|EMBL:RAS69302.1};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_02233};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_02233};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_02233};
KW   Protease {ECO:0000313|EMBL:RAS69302.1};
KW   Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_02233}.
FT   BINDING         39
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
FT   BINDING         180
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
FT   BINDING         193
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
FT   BINDING         197
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
SQ   SEQUENCE   292 AA;  33114 MW;  ACF13386B3EDBC4D CRC64;
     MKYALGPLLY FWPKQDVENF YQQAKESSAD IIYLGETVCS KRREMKPQHW FDIAKELSSA
     GKQVVLSTMA LFEAPSEINV LKKYIDNGDF AIEANDVSAI QMAHEKGIPF IVGPAVNTYN
     AYALQIFLKQ GMTRWCMPVE LSRDWLNNVL LQCEKIGIRN QFEVEVFSHG YLPLAYSARC
     FTARAENRAK DECETCCIKY PTGIQVSSQE GQSVFNLNGI QTQSGYCYNL MNDLPSMEGL
     VDVVRLSPLG VETFQHLNNF KQNEHGGHPT KLESQQCNGY WHQLAGLEVK NI
//
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