ID   UBIB_ACTP7              Reviewed;         544 AA.
AC   B3GZD0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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}; OrderedLocusNames=APP7_2071;
OS   Actinobacillus pleuropneumoniae serotype 7 (strain AP76).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=537457;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP76;
RA   Linke B., Buettner F., Martinez-Arias R., Goesmann A., Baltes N.,
RA   Tegetmeyer H., Singh M., Gerlach G.F.;
RT   "Genome and proteome analysis of A. pleuropneumoniae serotype 7.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis [regulation].
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00414}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00414}.
CC   -!- SIMILARITY: Belongs to the ABC1 family. UbiB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00414}.
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DR   EMBL; CP001091; ACE62723.1; -; Genomic_DNA.
DR   RefSeq; WP_005618418.1; NC_010939.1.
DR   AlphaFoldDB; B3GZD0; -.
DR   SMR; B3GZD0; -.
DR   EnsemblBacteria; ACE62723; ACE62723; APP7_2071.
DR   KEGG; apa:APP7_2071; -.
DR   HOGENOM; CLU_006533_0_0_6; -.
DR   OMA; RRDYKRV; -.
DR   BioCyc; APLE537457:APP7_RS10820-MON; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000001226; Chromosome.
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   3: Inferred from homology;
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_1000123887"
FT   TRANSMEM        522..540
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT   DOMAIN          123..505
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT   ACT_SITE        291
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         156
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
SQ   SEQUENCE   544 AA;  62866 MW;  67D07AE0B4BACB94 CRC64;
     MTCKNTRRLY QIITTFLRYG IDEIIPDIPL TRHARLGRKA LFWVRNQHKD QPFGVRLRLA
     LQELGPVWIK LGQMLSTRRD LFEPELAEQL ALLQDSVEPF DGKSARQIIE QALGGSLETW
     FDEFDEQALA SASIAQVHTA KFNQNQPLVG KDVVIKVIRP DIEPIIKADI ALMYRLASWV
     PRLSNDARRL RATEVVREYE KTLLDELDLT REMANAIRLR NNFENSEMLY VPEMYPDFCH
     KNVIVMERIY GILVSDVETL KANGTDMKLL AERGVQVFFT QVFRDSFFHA DMHAGNIFVN
     PNHPENPQYI GIDCGIVGTL NQNDKRYLAE SFVAFFNRDY RRVALMHVES GWTPADTDID
     AFEQAFREVC EPIFAKPLSE ISFGHVLLNL FNVAREFNME VQPQLVLLQK TLLYIEGLGR
     QVYPQLDLWQ TAKPFLQNWL NEQVGVKAIL RDLKQRAPQF REHFAEFPEA VFNALQQQKQ
     INFRLDELNK TLQAQGRQKS HNVRSIVSGV IILGVLWRFD DLPLWLSCGT LVTVLLVLLL
     QRKS