UBIV_ECOLI
ID UBIV_ECOLI Reviewed; 292 AA.
AC P45475; Q2M951;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Ubiquinone biosynthesis protein UbiV {ECO:0000255|HAMAP-Rule:MF_02233, ECO:0000305};
GN Name=ubiV {ECO:0000255|HAMAP-Rule:MF_02233, ECO:0000303|PubMed:31289180};
GN Synonyms=yhbV; OrderedLocusNames=b3159, JW5530;
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-39; CYS-180; CYS-193 AND CYS-197.
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 UbiU, is essential for the C6-hydroxylation
CC reaction in the oxygen-independent ubiquinone biosynthesis pathway.
CC {ECO:0000255|HAMAP-Rule:MF_02233, ECO:0000269|PubMed:31289180}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02233,
CC ECO:0000269|PubMed:31289180};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02233, ECO:0000269|PubMed:31289180}.
CC -!- SUBUNIT: Forms an heterodimer with UbiU. {ECO:0000255|HAMAP-
CC Rule:MF_02233, ECO:0000269|PubMed:31289180}.
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. UbiV subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02233, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA57962.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U18997; AAA57962.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76193.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77205.1; -; Genomic_DNA.
DR PIR; C65106; C65106.
DR RefSeq; NP_417628.2; NC_000913.3.
DR RefSeq; WP_001301318.1; NZ_STEB01000012.1.
DR AlphaFoldDB; P45475; -.
DR BioGRID; 4259276; 54.
DR DIP; DIP-12269N; -.
DR IntAct; P45475; 1.
DR STRING; 511145.b3159; -.
DR MEROPS; U32.A01; -.
DR jPOST; P45475; -.
DR PaxDb; P45475; -.
DR PRIDE; P45475; -.
DR EnsemblBacteria; AAC76193; AAC76193; b3159.
DR EnsemblBacteria; BAE77205; BAE77205; BAE77205.
DR GeneID; 949117; -.
DR KEGG; ecj:JW5530; -.
DR KEGG; eco:b3159; -.
DR PATRIC; fig|1411691.4.peg.3571; -.
DR EchoBASE; EB2643; -.
DR eggNOG; COG0826; Bacteria.
DR HOGENOM; CLU_056172_0_0_6; -.
DR InParanoid; P45475; -.
DR OMA; CCIKYPT; -.
DR PhylomeDB; P45475; -.
DR BioCyc; EcoCyc:G7653-MON; -.
DR UniPathway; UPA00232; -.
DR PRO; PR:P45475; -.
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_02233; UbiV; 1.
DR InterPro; IPR001539; Peptidase_U32.
DR InterPro; IPR043693; UbiV.
DR Pfam; PF01136; 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..292
FT /note="Ubiquinone biosynthesis protein UbiV"
FT /id="PRO_0000169459"
FT BINDING 39
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02233,
FT ECO:0000269|PubMed:31289180"
FT BINDING 180
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02233,
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_02233,
FT ECO:0000269|PubMed:31289180"
FT BINDING 197
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02233,
FT ECO:0000269|PubMed:31289180"
FT MUTAGEN 39
FT /note="C->A: Does not bind iron-sulfur cluster; when
FT associated with A-180; A-193 and A-197."
FT /evidence="ECO:0000269|PubMed:31289180"
FT MUTAGEN 180
FT /note="C->A: Alters ubiquinone synthesis in anaerobic
FT conditions. Does not bind iron-sulfur cluster; when
FT associated with A-39; A-193 and A-197."
FT /evidence="ECO:0000269|PubMed:31289180"
FT MUTAGEN 193
FT /note="C->A: Alters ubiquinone synthesis in anaerobic
FT conditions. Does not bind iron-sulfur cluster; when
FT associated with A-39; A-180 and A-197."
FT /evidence="ECO:0000269|PubMed:31289180"
FT MUTAGEN 197
FT /note="C->A: Does not bind iron-sulfur cluster; when
FT associated with A-39; A-180 and A-193."
FT /evidence="ECO:0000269|PubMed:31289180"
SQ SEQUENCE 292 AA; 32535 MW; AFCCD33E5A2D93B7 CRC64;
MKYSLGPVLW YWPKETLEEF YQQAATSSAD VIYLGEAVCS KRRATKVGDW LEMAKSLAGS
GKQIVLSTLA LVQASSELGE LKRYVENGEF LIEASDLGVV NMCAERKLPF VAGHALNCYN
AVTLKILLKQ GMMRWCMPVE LSRDWLVNLL NQCDELGIRN QFEVEVLSYG HLPLAYSARC
FTARSEDRPK DECETCCIKY PNGRNVLSQE NQQVFVLNGI QTMSGYVYNL GNELASMQGL
VDVVRLSPQG TDTFAMLDAF RANENGAAPL PLTANSDCNG YWRRLAGLEL QA
