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Database: UniProt
Entry: A0A318TDW0_9BRAD
LinkDB: A0A318TDW0_9BRAD
Original site: A0A318TDW0_9BRAD 
ID   A0A318TDW0_9BRAD        Unreviewed;       325 AA.
AC   A0A318TDW0;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Ubiquinone biosynthesis protein UbiU {ECO:0000256|HAMAP-Rule:MF_02232};
GN   Name=ubiU {ECO:0000256|HAMAP-Rule:MF_02232};
GN   ORFNames=BJ122_10975 {ECO:0000313|EMBL:PYF02944.1};
OS   Rhodopseudomonas faecalis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=99655 {ECO:0000313|EMBL:PYF02944.1, ECO:0000313|Proteomes:UP000248148};
RN   [1] {ECO:0000313|EMBL:PYF02944.1, ECO:0000313|Proteomes:UP000248148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 11668 {ECO:0000313|EMBL:PYF02944.1,
RC   ECO:0000313|Proteomes:UP000248148};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for O(2)-independent ubiquinone (coenzyme Q)
CC       biosynthesis. Together with UbiV, is essential for the C6-hydroxylation
CC       reaction in the oxygen-independent ubiquinone biosynthesis pathway.
CC       {ECO:0000256|HAMAP-Rule:MF_02232}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02232};
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_02232}.
CC   -!- SUBUNIT: Forms an heterodimer with UbiV. {ECO:0000256|HAMAP-
CC       Rule:MF_02232}.
CC   -!- SIMILARITY: Belongs to the peptidase U32 family. UbiU subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_02232}.
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:PYF02944.1}.
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DR   EMBL; QJTI01000009; PYF02944.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A318TDW0; -.
DR   OrthoDB; 9758184at2; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000248148; 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_02232; UbiU; 1.
DR   InterPro; IPR001539; Peptidase_U32.
DR   InterPro; IPR043692; UbiU.
DR   PANTHER; PTHR30217; PEPTIDASE U32 FAMILY; 1.
DR   PANTHER; PTHR30217:SF3; UBIQUINONE BIOSYNTHESIS PROTEIN UBIU; 1.
DR   Pfam; PF01136; Peptidase_U32; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_02232};
KW   Hydrolase {ECO:0000313|EMBL:PYF02944.1};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_02232};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_02232};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_02232};
KW   Protease {ECO:0000313|EMBL:PYF02944.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248148};
KW   Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_02232}.
FT   REGION          303..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..325
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         169
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02232"
FT   BINDING         176
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02232"
FT   BINDING         193
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02232"
FT   BINDING         232
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02232"
SQ   SEQUENCE   325 AA;  34873 MW;  44212509137B0A76 CRC64;
     MELICPAGTP SALRDAVAAG ADAVYCGFAD ETNARNFPGL NFSRSEMAES IAHAHQAGVK
     VLVAINTFAR AGSVGLWHSA VDDAVDAGAD AVIVADVGVM DYVARTHPQQ RLHISVQAAA
     ANPDAIRFYV DRFNAKRVVL PRVLSVPEIA AIGKEVNCET EVFIFGGLCV MEEGRCSLSS
     YATGKSPNMD GVCSPASHIQ YREENGMLVS RLGEFTINKF AAGEAAAYPT LCKGRYQTSE
     GCGYLFEDPT SLDATTMLPE LKNAGVCALK IEGRQRGRAY IERVVRTFRQ ALRALDAGQP
     IPTDELRGLS EGQSTTTGAY KKTWR
//
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