ID A0A0K6GT23_9NEIS Unreviewed; 301 AA.
AC A0A0K6GT23;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Ubiquinone biosynthesis protein UbiV {ECO:0000256|HAMAP-Rule:MF_02233};
GN Name=ubiV {ECO:0000256|HAMAP-Rule:MF_02233};
GN ORFNames=Ga0061063_0628 {ECO:0000313|EMBL:CUA81782.1};
OS Gulbenkiania indica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Gulbenkiania.
OX NCBI_TaxID=375574 {ECO:0000313|EMBL:CUA81782.1, ECO:0000313|Proteomes:UP000243535};
RN [1] {ECO:0000313|Proteomes:UP000243535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17901 {ECO:0000313|Proteomes:UP000243535};
RA Varghese N.;
RL Submitted (AUG-2015) 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}.
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DR EMBL; CYHA01000001; CUA81782.1; -; Genomic_DNA.
DR RefSeq; WP_055433425.1; NZ_LION01000001.1.
DR AlphaFoldDB; A0A0K6GT23; -.
DR STRING; 375574.GCA_001418035_00426; -.
DR OrthoDB; 8523349at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000243535; 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:CUA81782.1};
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:CUA81782.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000243535};
KW Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_02233}.
FT BINDING 44
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
FT BINDING 179
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
FT BINDING 192
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
FT BINDING 196
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
SQ SEQUENCE 301 AA; 32965 MW; 2C919FB8FEA1416B CRC64;
MTQLPLKLAL GPILYFWPRQ SVFDFYAEAA GWLVDTFYLG EVVCSRRQQL RTQDWIALAH
DLADTGKEVV LSCQALLESE SDLKRLRRLV ENGRVRIEAN DLGAARLAHS AGLPFVAGPH
LNVYNSETLA LMKRLGAWRW VPPVEMPADV LGTILSANPD IETEVFAWGR LPLAFSARCF
TARHYHLNKD DCQFRCLEHP DGLTLATREA QGFLTINGIQ TMSDGYQALL PHLSDMTAMG
VTGVRISPQS QGTAQVVAAF ADVVAGRLSP VDSLSALPGF TTGPLVDGYW RGMAGIAALE
V
//