ID   UBIB_PROST              Reviewed;         544 AA.
AC   O07443;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=Aminoglycoside acetyltransferase regulator;
DE   AltName: Full=Ubiquinone biosynthesis protein UbiB {ECO:0000255|HAMAP-Rule:MF_00414};
GN   Name=ubiB {ECO:0000255|HAMAP-Rule:MF_00414}; Synonyms=aarF;
OS   Providencia stuartii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Providencia.
OX   NCBI_TaxID=588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PR50;
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   [2]
RP   FUNCTION IN UBIQUINONE BIOSYNTHESIS, AND DISRUPTION PHENOTYPE.
RC   STRAIN=PR50;
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).
CC   -!- FUNCTION: Is probably a protein kinase regulator of UbiI activity which
CC       is involved in aerobic coenzyme Q (ubiquinone) biosynthesis. Required
CC       for the expression of 2'-N-acetyltransferase. {ECO:0000255|HAMAP-
CC       Rule:MF_00414, ECO:0000269|PubMed:10960098}.
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis [regulation].
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00414}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00414}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene fail to produce coenzyme
CC       Q8, and accumulate octaprenylphenol (OPP).
CC       {ECO:0000269|PubMed:10960098}.
CC   -!- SIMILARITY: Belongs to the ABC1 family. UbiB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00414}.
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DR   EMBL; AF002165; AAB96577.1; -; Genomic_DNA.
DR   PIR; T51162; T51162.
DR   AlphaFoldDB; O07443; -.
DR   SMR; O07443; -.
DR   STRING; 588.BGK56_10840; -.
DR   PRIDE; O07443; -.
DR   UniPathway; UPA00232; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniPathway.
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; Transferase; Transmembrane; Transmembrane helix;
KW   Ubiquinone biosynthesis.
FT   CHAIN           1..544
FT                   /note="Probable protein kinase UbiB"
FT                   /id="PRO_0000200713"
FT   TRANSMEM        499..519
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          123..500
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT   ACT_SITE        286
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT   BINDING         129..137
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT   BINDING         152
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
SQ   SEQUENCE   544 AA;  62599 MW;  E789A4E8185B4E96 CRC64;
     MTPGEIKRLY FIIRVFLSYG LDELIPKVKL TLPLRIGRFG FFWIKNQHKG KELGERLRLA
     LQELGPVWIK FGQMLSTRRD LFPLAIADQL SLLQDKVASF DGKLARRYIE ESLGGPLEQW
     FDDFDEKALA SASIAQVHTA KLKENGKEVV LKVIRPDILP VIKADVKLMY RIANWVPLLP
     DGRRLRPKEV VREYEKTLID ELNLLRESAN AIQLRRNFEN SSMLYVPEVY ADYCRENVMV
     MERIYGIPVS DIAALKAQGT NMKILAERGV KVFFTQVFRD SFFHADMHPG NIFVSYEHPE
     DPLYIGIDCG IVGSLNKEDK RYLAENFIAF FNRDYRKVAE LHVDSGWVPA DTNVEDFEFA
     IRTVCEPIFE KPLAEISFGH VLLNLFNTAR RFNMEVQPQL VLLQKTLLYI EGLGRQLYPQ
     LDLWKTAKPF LEDWVHSQVG IPAITQALKE KAPYWAEKMP EIPDLIYGAL RQHKFLQSNI
     EQLSEQLKQQ RNKQRKSQYL LGIGATLILC GSLFFISASN RMAIAFMSAG ALSWIIGWYK
     SGKS