ID K4KPK2_SIMAS Unreviewed; 289 AA.
AC K4KPK2;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Ubiquinone biosynthesis protein UbiV {ECO:0000256|HAMAP-Rule:MF_02233};
GN Name=ubiV {ECO:0000256|HAMAP-Rule:MF_02233};
GN OrderedLocusNames=M5M_15055 {ECO:0000313|EMBL:AFV00146.1};
OS Simiduia agarivorans (strain DSM 21679 / JCM 13881 / BCRC 17597 / SA1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Simiduia.
OX NCBI_TaxID=1117647 {ECO:0000313|EMBL:AFV00146.1, ECO:0000313|Proteomes:UP000000466};
RN [1] {ECO:0000313|EMBL:AFV00146.1, ECO:0000313|Proteomes:UP000000466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21679 / JCM 13881 / BCRC 17597 / SA1
RC {ECO:0000313|Proteomes:UP000000466};
RX PubMed=23405302; DOI=10.1128/genomeA.00039-12;
RA Lin S.Y., Shieh W.Y., Chen J.S., Tang S.L.;
RT "Complete genome sequence of Simiduia agarivorans SA1(T), a marine
RT bacterium able to degrade a variety of polysaccharides.";
RL Genome Announc. 1:E00039-E00039(2013).
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; CP003746; AFV00146.1; -; Genomic_DNA.
DR RefSeq; WP_015048298.1; NZ_ATUQ01000010.1.
DR AlphaFoldDB; K4KPK2; -.
DR STRING; 1117647.M5M_15055; -.
DR KEGG; saga:M5M_15055; -.
DR eggNOG; COG0826; Bacteria.
DR HOGENOM; CLU_056172_0_0_6; -.
DR OrthoDB; 8523349at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000000466; Chromosome.
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:AFV00146.1};
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:AFV00146.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000466};
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 176
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
FT BINDING 189
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"
SQ SEQUENCE 289 AA; 31997 MW; 3D12247E24D49842 CRC64;
MKLSLGPIQY FWSHKDVLEF YARMIETPVN TLYLGEVVCG KRRELSPIQW IDLARQLASS
CGKEIILSTM TLIESGADLK GVKRLCDNEG LLVEANDIAA IHYLSEKKLP FVAGPAINIY
NAQSLQFLMS QGLKRWVVPV ELGQQQLRAA LTPLKVKPEI EVLAWGRLPL AYSARCFTAR
HHGVKKDDCA FVCQQYPAGL QLKSQESQSL FTLNGIATLS GMPVNLLNHH ASLTDTGVSH
ARISPEWEQT EIVIETFYNA LRGSSTASLA GGTDGYWRGQ PGIDLIARE
//