ID   UBIB_SHEON              Reviewed;         549 AA.
AC   Q8E9R5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=SO_4201;
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN57173.1; -; Genomic_DNA.
DR   RefSeq; NP_719729.1; NC_004347.2.
DR   RefSeq; WP_011073884.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8E9R5; -.
DR   SMR; Q8E9R5; -.
DR   STRING; 211586.SO_4201; -.
DR   PaxDb; Q8E9R5; -.
DR   PRIDE; Q8E9R5; -.
DR   KEGG; son:SO_4201; -.
DR   PATRIC; fig|211586.12.peg.4057; -.
DR   eggNOG; COG0661; Bacteria.
DR   HOGENOM; CLU_006533_0_0_6; -.
DR   OMA; RRDYKRV; -.
DR   OrthoDB; 678616at2; -.
DR   PhylomeDB; Q8E9R5; -.
DR   BioCyc; SONE211586:G1GMP-3874-MON; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000008186; 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; 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; 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; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix; Ubiquinone biosynthesis.
FT   CHAIN           1..549
FT                   /note="Probable protein kinase UbiB"
FT                   /id="PRO_1000123926"
FT   TRANSMEM        498..518
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT   TRANSMEM        520..540
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT   DOMAIN          123..501
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT   ACT_SITE        287
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   549 AA;  63246 MW;  757D9E8A80AD58D5 CRC64;
     MTLASIRRGY HVIKTLLQYG LDDVLPPKMT PWYFTLARNS LFWIRNKHKD KSGGERLKLA
     MQELGPVYIK LGQMLSTRRD LLSDEWATEL AMLQDKVPPF DGALARLAIE AELKAPIETF
     FDDFNETPLA SASISQVHTA TLKSNGKAVV LKVLRPNVET KIQADLLLMS QTAKVIDYLL
     GEGNRLRPAE VIEDYRVTIL GELNLKLEAL NAIKLRNNFI DSDALYIPYV YEEFCYPRLM
     VMERIYGIPV SDIVALKAQG TNFKLLAERG VELFFTQVFR DNFFHADMHP GNIFISRENP
     ENPYYIGLDC GIMGTLSEVD KRYLAENFLA FFNRDYHRIA QLYIESGWVS EKTDLQAFEQ
     AIKVVCEPMF NKPLDEISFG HVLLELFRTA RHFDIVVQPQ LVLLEKTLLY IEGLGRQLYP
     QLDLWQTAKP FLEQWMAEQV GPKAMFKKVS TKLPYWSDKL PEFPELIYDN LKLGRKLLSS
     QQQMLDKYLK YQQQAHKSNY LLITSAILLI CGTLLFNQDA TLLSPYVCLI SGAVLWIIGW
     RSRPKNRKF