ID F2BER0_9NEIS Unreviewed; 369 AA.
AC F2BER0;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Ubiquinone biosynthesis protein UbiU {ECO:0000256|HAMAP-Rule:MF_02232};
GN Name=ubiU {ECO:0000256|HAMAP-Rule:MF_02232};
GN ORFNames=HMPREF9123_2217 {ECO:0000313|EMBL:EGF09965.1};
OS Neisseria bacilliformis ATCC BAA-1200.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=888742 {ECO:0000313|EMBL:EGF09965.1, ECO:0000313|Proteomes:UP000004105};
RN [1] {ECO:0000313|EMBL:EGF09965.1, ECO:0000313|Proteomes:UP000004105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1200 {ECO:0000313|EMBL:EGF09965.1,
RC ECO:0000313|Proteomes:UP000004105};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (FEB-2011) 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:EGF09965.1}.
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DR EMBL; AFAY01000046; EGF09965.1; -; Genomic_DNA.
DR AlphaFoldDB; F2BER0; -.
DR STRING; 267212.GCA_001063965_00372; -.
DR HOGENOM; CLU_011540_3_2_4; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000004105; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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:EGF09965.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000004105};
KW Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_02232}.
FT BINDING 207
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02232"
FT BINDING 214
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02232"
FT BINDING 231
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02232"
FT BINDING 270
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02232"
SQ SEQUENCE 369 AA; 40424 MW; 74CCF6D78A7F7886 CRC64;
MTALLSDFNK KTASAAGGGR AFFTTIQHVQ GTQMTNRIPE LVCPSGNLPA LKTAVDNGAD
TVYMGLKDAT NARNFPGLNF DMNSARAGVE YAHARGRSVL MAINTFAQAG QVERWYAAVD
TAAQLGADAV IVADPAVMAY AAKRYPDLRL HMSVQGSATN YEAVNLMKDL FNVRRAVLPR
VLTIDQVKHV IDHTDVEIEV FGFGSLCVMV EGRCILSSYA TGESPNMQGV CSPAKAVRWE
QLPDRMDVRL NHILIDRYKP NEPAGYPTLC KGRFEVNDET YYALEEPTSL NILEMLPEII
KIGVAAVKIE GRQRSPMYTA QVTKSLRQAL DAAAADPSHF RVNPAWSKAL DKVSEGHQTT
LGAYSRPWK
//
