ID   UBIB_SALCH              Reviewed;         546 AA.
AC   Q57HN6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=SCH_3870;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(2005).
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}; Multi-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; AE017220; AAX67776.1; -; Genomic_DNA.
DR   RefSeq; WP_000187559.1; NC_006905.1.
DR   AlphaFoldDB; Q57HN6; -.
DR   SMR; Q57HN6; -.
DR   PRIDE; Q57HN6; -.
DR   EnsemblBacteria; AAX67776; AAX67776; SCH_3870.
DR   KEGG; sec:SCH_3870; -.
DR   HOGENOM; CLU_006533_0_0_6; -.
DR   OMA; RRDYKRV; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000000538; 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..546
FT                   /note="Probable protein kinase UbiB"
FT                   /id="PRO_1000050053"
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"
SQ   SEQUENCE   546 AA;  63239 MW;  362873022A808F1A CRC64;
     MTPGEVRRLY FIIRTFLSYG LDELIPRMRL TLPLRLWRYS LFWMPNRHKD KLLGERLRLA
     LQELGPVWIK FGQMLSTRRD LFPPQIADQL ALLQDKVAPF DGRLAKAQIE EAMGGLPVEA
     WFDDFDIQPL ASASIAQVHT ARLKSNGKEV VIKVIRPDIL PVIQADLKLI YRLARWVPRL
     LPDGRRLRPT EVVREYEKTL IDELNLLRES ANAIQLRRNF ENSPMLYIPE VYSDYCSQNM
     MVMERIYGIP VSDVAALEKN GTNMKLLAER GVKVFFTQVF RDSFFHADMH PGNIFVSHEH
     PENPQYIGID CGIVGSLNKE DKRYLAENFI AFFNRDYRKV AELHVDSGWV PPDTNVEDFE
     FAIRTVCEPI FEKPLAEISF GHVLLNLFNT ARRFNMEVQP QLVLLQKTLL YVEGVGRQLY
     PQLDLWKTAK PFLESWIKDQ VGIPALTRAL KEKAPFWVEK MPEIPELVYD SLRQGKYLQH
     SVDKIARELQ VNHVRQSQSR YLLGIGATLL LSGSFLLVNR PEWGLMPGWL MVGGVVVWLV
     GWRKTR