ID UBIB_TOLAT Reviewed; 543 AA.
AC C4L962;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
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=Tola_0331;
OS Tolumonas auensis (strain DSM 9187 / TA4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Tolumonas.
OX NCBI_TaxID=595494;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9187 / TA4;
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., Spring S.,
RA Beller H.;
RT "Complete sequence of Tolumonas auensis DSM 9187.";
RL Submitted (MAY-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}; 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; CP001616; ACQ91961.1; -; Genomic_DNA.
DR RefSeq; WP_012728560.1; NC_012691.1.
DR AlphaFoldDB; C4L962; -.
DR SMR; C4L962; -.
DR STRING; 595494.Tola_0331; -.
DR KEGG; tau:Tola_0331; -.
DR eggNOG; COG0661; Bacteria.
DR HOGENOM; CLU_006533_0_0_6; -.
DR OrthoDB; 9795390at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000009073; Chromosome.
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 NCBIfam; TIGR01982; UbiB; 1.
DR PANTHER; PTHR10566; CHAPERONE-ACTIVITY OF BC1 COMPLEX CABC1 -RELATED; 1.
DR PANTHER; PTHR10566:SF129; PROTEIN KINASE UBIB-RELATED; 1.
DR Pfam; PF03109; ABC1; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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..543
FT /note="Probable protein kinase UbiB"
FT /id="PRO_1000206017"
FT TRANSMEM 499..519
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00414"
FT TRANSMEM 521..541
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 543 AA; 63191 MW; 580C7B06174AA5DE CRC64;
MILREWRRFY TIGSVLLRHG LDELIPRHWQ PWPVRLFRRS LFWLRNRYPE QSRGARLRHA
FEGLGPVFIK FGQMLSTRRD LLPPDLAEEL AMLQDRVPSF DGQLAREQIE QALGQPIEAL
FADFDQQPLA SASVAQVHTA RLKENNAEIV IKVIRPDIKP VINDDIRLMR LCAKIVAFLI
PNNRLRPVEV IEEYRRTLLD ELNLMSEAAN AIQLRRNFEN SSHLYVPLVY SDYCRESVLV
MERIYGIPVS DRAALEANGT DLKLLAERGV EVFFTQVFRD SFFHADMHPG NVFVSYEHPH
DPQWIGIDCG IVGTLNRQDK RYLAENFLAF FNRDYRKVAE LHVQSGWVPP DTKVEEFESA
LRTVLEPIFA KPLAEISFGQ VLLNLFNTAR RFNMHVQPQL VLLQKTLLYI EGLGRHLYPQ
LDLWQTAKPF LEHWMRQQIG PKAAWRAIKE KAPFWAEKLP DMPDLIYDTL TQVQHQQHMV
KGLYQQYHQQ HRRHAQARFL LGAGATLLLG SILLLPTHEQ LASAGLTISI ICWLNGWWKI
SRR
//
