UBIB_ECOLI
ID UBIB_ECOLI Reviewed; 546 AA.
AC P0A6A0; P27853; P27854; P27855; P76764; Q2M8E0;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Probable protein kinase UbiB {ECO:0000255|HAMAP-Rule:MF_00414};
DE EC=2.7.-.- {ECO:0000255|HAMAP-Rule:MF_00414};
DE AltName: Full=Ubiquinone biosynthesis protein UbiB {ECO:0000255|HAMAP-Rule:MF_00414};
GN Name=ubiB {ECO:0000255|HAMAP-Rule:MF_00414};
GN Synonyms=aarF, yigQ, yigR, yigS; OrderedLocusNames=b3835, JW3812;
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=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 439-536.
RX PubMed=3309887; DOI=10.1093/nar/15.17.6827;
RA Mizuno T.;
RT "Random cloning of bent DNA segments from Escherichia coli chromosome and
RT primary characterization of their structures.";
RL Nucleic Acids Res. 15:6827-6841(1987).
RN [5]
RP FUNCTION IN UBIQUINONE BIOSYNTHESIS, AND DISRUPTION PHENOTYPE.
RX PubMed=9422602; DOI=10.1128/jb.180.1.128-135.1998;
RA Macinga D.R., Cook G.M., Poole R.K., Rather P.N.;
RT "Identification and characterization of aarF, a locus required for
RT production of ubiquinone in Providencia stuartii and Escherichia coli and
RT for expression of 2'-N-acetyltransferase in P. stuartii.";
RL J. Bacteriol. 180:128-135(1998).
RN [6]
RP FUNCTION IN UBIQUINONE BIOSYNTHESIS, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / RM1734;
RX PubMed=10960098; DOI=10.1128/jb.182.18.5139-5146.2000;
RA Poon W.W., Davis D.E., Ha H.T., Jonassen T., Rather P.N., Clarke C.F.;
RT "Identification of Escherichia coli ubiB, a gene required for the first
RT monooxygenase step in ubiquinone biosynthesis.";
RL J. Bacteriol. 182:5139-5146(2000).
RN [7]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [8]
RP PROBABLE FUNCTION.
RC STRAIN=K12;
RX PubMed=23709220; DOI=10.1074/jbc.m113.480368;
RA Hajj Chehade M., Loiseau L., Lombard M., Pecqueur L., Ismail A., Smadja M.,
RA Golinelli-Pimpaneau B., Mellot-Draznieks C., Hamelin O., Aussel L.,
RA Kieffer-Jaquinod S., Labessan N., Barras F., Fontecave M., Pierrel F.;
RT "ubiI, a new gene in Escherichia coli coenzyme Q biosynthesis, is involved
RT in aerobic C5-hydroxylation.";
RL J. Biol. Chem. 288:20085-20092(2013).
CC -!- FUNCTION: Is probably a protein kinase regulator of UbiI activity which
CC is involved in aerobic coenzyme Q (ubiquinone) biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00414, ECO:0000269|PubMed:10960098,
CC ECO:0000269|PubMed:9422602}.
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis [regulation].
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00414, ECO:0000269|PubMed:15919996}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_00414, ECO:0000269|PubMed:15919996}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene fail to produce coenzyme
CC Q8, and accumulate octaprenylphenol (OPP).
CC {ECO:0000269|PubMed:10960098, ECO:0000269|PubMed:9422602}.
CC -!- SIMILARITY: Belongs to the ABC1 family. UbiB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00414}.
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DR EMBL; M87049; AAA67630.2; ALT_FRAME; Genomic_DNA.
DR EMBL; M87049; AAA67631.1; ALT_FRAME; Genomic_DNA.
DR EMBL; M87049; AAA67632.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC76838.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77466.1; -; Genomic_DNA.
DR EMBL; X05967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; D65188; D65188.
DR RefSeq; NP_418279.1; NC_000913.3.
DR RefSeq; WP_000187530.1; NZ_STEB01000021.1.
DR AlphaFoldDB; P0A6A0; -.
DR SMR; P0A6A0; -.
DR BioGRID; 4260948; 361.
DR DIP; DIP-35858N; -.
DR IntAct; P0A6A0; 13.
DR STRING; 511145.b3835; -.
DR jPOST; P0A6A0; -.
DR PaxDb; P0A6A0; -.
DR PRIDE; P0A6A0; -.
DR DNASU; 948322; -.
DR EnsemblBacteria; AAC76838; AAC76838; b3835.
DR EnsemblBacteria; BAE77466; BAE77466; BAE77466.
DR GeneID; 66672257; -.
DR GeneID; 948322; -.
DR KEGG; ecj:JW3812; -.
DR KEGG; eco:b3835; -.
DR PATRIC; fig|1411691.4.peg.2873; -.
DR EchoBASE; EB1443; -.
DR eggNOG; COG0661; Bacteria.
DR HOGENOM; CLU_006533_0_0_6; -.
DR InParanoid; P0A6A0; -.
DR OMA; RRDYKRV; -.
DR PhylomeDB; P0A6A0; -.
DR BioCyc; EcoCyc:2-OCTAPRENYLPHENOL-HYDROX-MON; -.
DR UniPathway; UPA00232; -.
DR PRO; PR:P0A6A0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010795; P:regulation of ubiquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IMP:EcoCyc.
DR CDD; cd13972; UbiB; 1.
DR HAMAP; MF_00414; UbiB; 1.
DR InterPro; IPR004147; ABC1_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR010232; UbiB.
DR InterPro; IPR045308; UbiB_bact.
DR Pfam; PF03109; ABC1; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR TIGRFAMs; TIGR01982; UbiB; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Ubiquinone biosynthesis.
FT CHAIN 1..546
FT /note="Probable protein kinase UbiB"
FT /id="PRO_0000200703"
FT TRANSMEM 501..521
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT TRANSMEM 522..542
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT DOMAIN 124..502
FT /note="Protein kinase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT ACT_SITE 288
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT BINDING 130..138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT BINDING 153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT CONFLICT 525
FT /note="L -> V (in Ref. 4; X05967)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 546 AA; 63203 MW; D66C8AD50C05B4EC CRC64;
MTPGEVRRLY FIIRTFLSYG LDELIPKMRI TLPLRLWRYS LFWMPNRHKD KLLGERLRLA
LQELGPVWIK FGQMLSTRRD LFPPHIADQL ALLQDKVAPF DGKLAKQQIE AAMGGLPVEA
WFDDFEIKPL ASASIAQVHT ARLKSNGKEV VIKVIRPDIL PVIKADLKLI YRLARWVPRL
LPDGRRLRPT EVVREYEKTL IDELNLLRES ANAIQLRRNF EDSPMLYIPE VYPDYCSEGM
MVMERIYGIP VSDVAALEKN GTNMKLLAER GVQVFFTQVF RDSFFHADMH PGNIFVSYEH
PENPKYIGID CGIVGSLNKE DKRYLAENFI AFFNRDYRKV AELHVDSGWV PPDTNVEEFE
FAIRTVCEPI FEKPLAEISF GHVLLNLFNT ARRFNMEVQP QLVLLQKTLL YVEGVGRQLY
PQLDLWKTAK PFLESWIKDQ VGIPALVRAF KEKAPFWVEK MPELPELVYD SLRQGKYLQH
SVDKIARELQ SNHVRQGQSR YFLGIGATLV LSGTFLLVSR PEWGLMPGWL MAGGLIAWFV
GWRKTR
