ID A0A220S0U4_9NEIS Unreviewed; 334 AA.
AC A0A220S0U4;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Ubiquinone biosynthesis protein UbiU {ECO:0000256|HAMAP-Rule:MF_02232};
GN Name=ubiU {ECO:0000256|HAMAP-Rule:MF_02232};
GN ORFNames=BG910_04575 {ECO:0000313|EMBL:ASK27110.1};
OS Neisseria chenwenguii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=1853278 {ECO:0000313|EMBL:ASK27110.1, ECO:0000313|Proteomes:UP000198238};
RN [1] {ECO:0000313|EMBL:ASK27110.1, ECO:0000313|Proteomes:UP000198238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10023 {ECO:0000313|EMBL:ASK27110.1,
RC ECO:0000313|Proteomes:UP000198238};
RA Zhang G.;
RT "Neisseria chenwenguii sp. nov., isolated from the intestinal contents of
RT Tibetan Plateau Pika in Yushu, Qinghai Province, China.";
RL Submitted (JUN-2017) 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}.
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DR EMBL; CP022278; ASK27110.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A220S0U4; -.
DR KEGG; nei:BG910_04575; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000198238; 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_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.
DR PROSITE; PS01276; PEPTIDASE_U32; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_02232};
KW Hydrolase {ECO:0000313|EMBL:ASK27110.1};
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:ASK27110.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198238};
KW Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_02232}.
FT BINDING 172
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02232"
FT BINDING 179
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02232"
FT BINDING 196
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02232"
FT BINDING 235
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02232"
SQ SEQUENCE 334 AA; 36420 MW; C3764C4588AAD16F CRC64;
MAIPELVCPA GNLAMLKTAV DNGADTVYMG LKDATNARNF PGLNFDLKTA AEGVAYAHAR
GRQVLMAINT FAQAGQVAQW RKAVDTAADL GADAVILADP ALMAYACEKH PKLRLHMSVQ
GSATNYEAIN LMKELFGVRR AVLPRVLTID QVKHVADNTD VEIEVFGFGS LCVMVEGRCI
LSSYATGESP NMQGVCSPAK AVRWEQLPDR MNVRLNNILI DHFNPDEPAG YPTLCKGRFE
VEDETYYALE EPTSLNVLEV LPELLKISVS AIKVEGRQRS QMYTAQVTRA LRQALDAAAA
DPQHYRVSPA WSGALGKVSE GHQSTLGAYS RPWK
//
