ID   UBIU_ECOLI              Reviewed;         331 AA.
AC   P45527; Q2M952;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Ubiquinone biosynthesis protein UbiU {ECO:0000255|HAMAP-Rule:MF_02232, ECO:0000305};
GN   Name=ubiU {ECO:0000255|HAMAP-Rule:MF_02232, ECO:0000303|PubMed:31289180};
GN   Synonyms=yhbU; OrderedLocusNames=b3158, JW3127;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [3]
RP   FUNCTION, COFACTOR, PATHWAY, SUBUNIT, DISRUPTION PHENOTYPE, AND MUTAGENESIS
RP   OF CYS-169; CYS-176; CYS-193 AND CYS-232.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=31289180; DOI=10.1128/mbio.01319-19;
RA   Pelosi L., Vo C.D., Abby S.S., Loiseau L., Rascalou B., Hajj Chehade M.,
RA   Faivre B., Gousse M., Chenal C., Touati N., Binet L., Cornu D., Fyfe C.D.,
RA   Fontecave M., Barras F., Lombard M., Pierrel F.;
RT   "Ubiquinone biosynthesis over the entire O2 range: characterization of a
RT   conserved O2-independent pathway.";
RL   MBio 10:E01319-E01319(2019).
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:0000255|HAMAP-Rule:MF_02232, ECO:0000269|PubMed:31289180}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02232,
CC         ECO:0000269|PubMed:31289180};
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_02232, ECO:0000269|PubMed:31289180}.
CC   -!- SUBUNIT: Forms an heterodimer with UbiV. {ECO:0000255|HAMAP-
CC       Rule:MF_02232, ECO:0000269|PubMed:31289180}.
CC   -!- INTERACTION:
CC       P45527; P0A6F5: groEL; NbExp=4; IntAct=EBI-561157, EBI-543750;
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant is unable to synthesize
CC       ubiquinone under strict anaerobic conditions. Mutant shows normal
CC       levels of ubiquinone after aerobic growth.
CC       {ECO:0000269|PubMed:31289180}.
CC   -!- SIMILARITY: Belongs to the peptidase U32 family. UbiU subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_02232, ECO:0000305}.
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DR   EMBL; U18997; AAA57961.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76192.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77204.1; -; Genomic_DNA.
DR   PIR; B65106; B65106.
DR   RefSeq; NP_417627.1; NC_000913.3.
DR   RefSeq; WP_001311152.1; NZ_LN832404.1.
DR   AlphaFoldDB; P45527; -.
DR   SMR; P45527; -.
DR   BioGRID; 4259275; 98.
DR   DIP; DIP-12268N; -.
DR   IntAct; P45527; 12.
DR   STRING; 511145.b3158; -.
DR   jPOST; P45527; -.
DR   PaxDb; P45527; -.
DR   PRIDE; P45527; -.
DR   EnsemblBacteria; AAC76192; AAC76192; b3158.
DR   EnsemblBacteria; BAE77204; BAE77204; BAE77204.
DR   GeneID; 949115; -.
DR   KEGG; ecj:JW3127; -.
DR   KEGG; eco:b3158; -.
DR   PATRIC; fig|1411691.4.peg.3572; -.
DR   EchoBASE; EB2642; -.
DR   eggNOG; COG0826; Bacteria.
DR   HOGENOM; CLU_011540_3_2_6; -.
DR   InParanoid; P45527; -.
DR   OMA; HVAINTF; -.
DR   PhylomeDB; P45527; -.
DR   BioCyc; EcoCyc:G7652-MON; -.
DR   UniPathway; UPA00232; -.
DR   PRO; PR:P45527; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032150; P:ubiquinone biosynthetic process from chorismate; IMP:EcoCyc.
DR   HAMAP; MF_02232; UbiU; 1.
DR   InterPro; IPR001539; Peptidase_U32.
DR   InterPro; IPR036206; ThiamineP_synth_sf.
DR   InterPro; IPR043692; UbiU.
DR   Pfam; PF01136; Peptidase_U32; 1.
DR   SUPFAM; SSF51391; SSF51391; 1.
DR   PROSITE; PS01276; PEPTIDASE_U32; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding; Reference proteome;
KW   Ubiquinone biosynthesis.
FT   CHAIN           1..331
FT                   /note="Ubiquinone biosynthesis protein UbiU"
FT                   /id="PRO_0000028525"
FT   BINDING         169
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02232,
FT                   ECO:0000269|PubMed:31289180"
FT   BINDING         176
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02232,
FT                   ECO:0000269|PubMed:31289180"
FT   BINDING         193
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02232,
FT                   ECO:0000269|PubMed:31289180"
FT   BINDING         232
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02232,
FT                   ECO:0000269|PubMed:31289180"
FT   MUTAGEN         169
FT                   /note="C->A: Decreases iron-sulfur binding; when associated
FT                   with A-176."
FT                   /evidence="ECO:0000269|PubMed:31289180"
FT   MUTAGEN         176
FT                   /note="C->A: Alters ubiquinone synthesis in anaerobic
FT                   conditions. Decreases iron-sulfur binding; when associated
FT                   with A-169."
FT                   /evidence="ECO:0000269|PubMed:31289180"
FT   MUTAGEN         193
FT                   /note="C->A: Decreases iron-sulfur binding; when associated
FT                   with A-232."
FT                   /evidence="ECO:0000269|PubMed:31289180"
FT   MUTAGEN         232
FT                   /note="C->A: Decreases iron-sulfur binding; when associated
FT                   with A-193."
FT                   /evidence="ECO:0000269|PubMed:31289180"
SQ   SEQUENCE   331 AA;  37047 MW;  2AFDED5929C4CFA7 CRC64;
     MELLCPAGNL PALKAAIENG ADAVYIGLKD DTNARHFAGL NFTEKKLQEA VSFVHQHRRK
     LHIAINTFAH PDGYARWQRA VDMAAQLGAD ALILADLAML EYAAERYPHI ERHVSVQASA
     TNEEAINFYH RHFDVARVVL PRVLSIHQVK QLARVTPVPL EVFAFGSLCI MSEGRCYLSS
     YLTGESPNTI GACSPARFVR WQQTPQGLES RLNEVLIDRY QDGENAGYPT LCKGRYLVDG
     ERYHALEEPT SLNTLELLPE LMAANIASVK IEGRQRSPAY VSQVAKVWRQ AIDRCKADPQ
     NFVPQSAWME TLGSMSEGTQ TTLGAYHRKW Q