ID   UBIB_ACIET              Reviewed;         521 AA.
AC   B9ME24;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=Dtpsy_0799;
OS   Acidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Diaphorobacter.
OX   NCBI_TaxID=535289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TPSY;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Coates J.D.;
RT   "Complete sequence of Diaphorobacter sp. TPSY.";
RL   Submitted (JAN-2009) 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; CP001392; ACM32278.1; -; Genomic_DNA.
DR   RefSeq; WP_012655778.1; NC_011992.1.
DR   AlphaFoldDB; B9ME24; -.
DR   SMR; B9ME24; -.
DR   STRING; 535289.Dtpsy_0799; -.
DR   EnsemblBacteria; ACM32278; ACM32278; Dtpsy_0799.
DR   KEGG; dia:Dtpsy_0799; -.
DR   eggNOG; COG0661; Bacteria.
DR   HOGENOM; CLU_006533_0_0_4; -.
DR   OMA; RRDYKRV; -.
DR   OrthoDB; 678616at2; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000000450; 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..521
FT                   /note="Probable protein kinase UbiB"
FT                   /id="PRO_1000134814"
FT   TRANSMEM        496..516
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT   DOMAIN          119..497
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         125..133
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT   BINDING         151
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
SQ   SEQUENCE   521 AA;  59955 MW;  5FBB88630F7CD536 CRC64;
     MSRFARGITI VWVVLRYGLD ELVLSTFRQP WLRAVTRVIT FGRKLDAPRG QRLREALESL
     GPIFVKFGQV LSTRRDLMPP DIADELALLQ DRVPPFDPDV AIATIERAFR RPIGEVFVSF
     DRQPVASASI AQVHFAVIRD RQGHAREVAV KVLRPGMLPV IDKDLALMRM MAGWVESLSA
     DGKRLKPREV VAEFDNYLHD ELDLVREAAN AAQLRRNMQG LDLVLIPEVF WDFCHAEVLV
     MERMKGVPIN QVERLRSAGV DIPKLARDGV TIFFTQVFRD GFFHADMHPG NIQVSLAPET
     FGRYISLDFG IVGTLTEFDK EYLAQNFTAF FRRDYKRVAE LHIESGWVPA HTRVNELEAA
     IRTVCEPYFD RPLKEISLGM VLLRLFQTSR RFQVEIQPQL VLLQKTLLNI EGLGRQLDPD
     LDLWSTAKPF LEKWMLDQLG PQRLWRELRA EAPHYAKILP DLPRLLHDFL RQRPHDNRGD
     LQELLATQKR TNRLLQSIIY GGLGFVLGLL VMQLFVRVRI F