UBIB_DELAS
ID UBIB_DELAS Reviewed; 521 AA.
AC A9BP42;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Daci_5458;
OS Delftia acidovorans (strain DSM 14801 / SPH-1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=398578;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL Submitted (NOV-2007) 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; CP000884; ABX38087.1; -; Genomic_DNA.
DR RefSeq; WP_012207256.1; NC_010002.1.
DR AlphaFoldDB; A9BP42; -.
DR SMR; A9BP42; -.
DR STRING; 398578.Daci_5458; -.
DR PRIDE; A9BP42; -.
DR EnsemblBacteria; ABX38087; ABX38087; Daci_5458.
DR KEGG; dac:Daci_5458; -.
DR eggNOG; COG0661; Bacteria.
DR HOGENOM; CLU_006533_0_0_4; -.
DR OMA; RRDYKRV; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000000784; 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; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Ubiquinone biosynthesis.
FT CHAIN 1..521
FT /note="Probable protein kinase UbiB"
FT /id="PRO_1000123901"
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; 60386 MW; AA7B6DFA647EB66E CRC64;
MSRFLRGLTI LWVVFRYGLD ELVLSSFEHP WMRRARAVLT LGRRLDKPRG QRLREALEEL
GPIFVKFGQV LSTRSDLMPP DVAEELARLQ DRVPPFDSQI AVDTIERAFR KKLDQIFVSF
EREPVASASI AQVHFAVISD RNGVQRDVAV KVLRPGMKTV IDKDLALMHM MARWVERLSA
DGKRLKPRQV VAEFDNYLHD ELDLIREASN AAQLRRNMEG LDLVLIPEVY WDFCRSDVMV
MQRMTGVPIS QVERLREAGV DIPKLARDGV TIFFTQVFRD GFFHADMHPG NIMVSLEPET
FGRYISLDFG IVGTLTEYDK EYLAQNFTAF FRRDYKRVAE LHIESGWVPP STRVDELEAA
IRAVCEPYFD RPLAEISLGM VLMRLFQTSR RFQVEIQPQL VLLQKTLLNI EGLGRQLDPN
LDLWSTAKPF LEKWMLDQMG PQRLWRELLA EAPRYAKLIP ELPRLIHRRL TRNSGEHDEL
LKELLQQQKL TNRLLQAIVS AGIGFVIALI LLQLVVRLRW Y