ID G4E6Q2_9GAMM Unreviewed; 556 AA.
AC G4E6Q2;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Probable protein kinase UbiB {ECO:0000256|HAMAP-Rule:MF_00414};
DE EC=2.7.-.- {ECO:0000256|HAMAP-Rule:MF_00414};
DE AltName: Full=Ubiquinone biosynthesis protein UbiB {ECO:0000256|HAMAP-Rule:MF_00414};
GN Name=ubiB {ECO:0000256|HAMAP-Rule:MF_00414};
GN ORFNames=ThisiDRAFT_1981 {ECO:0000313|EMBL:EGZ44675.1};
OS Thiorhodospira sibirica ATCC 700588.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thiorhodospira.
OX NCBI_TaxID=765914 {ECO:0000313|EMBL:EGZ44675.1};
RN [1] {ECO:0000313|EMBL:EGZ44675.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700588 {ECO:0000313|EMBL:EGZ44675.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J.,
RA Frigaard N.-U., Bryant D., Woyke T.;
RT "The draft genome of Thiorhodospira sibirica ATCC 700588.";
RL Submitted (SEP-2011) 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:0000256|HAMAP-Rule:MF_00414}.
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis [regulation].
CC {ECO:0000256|ARBA:ARBA00005020, ECO:0000256|HAMAP-Rule:MF_00414}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00414};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00414}.
CC -!- SIMILARITY: Belongs to the ABC1 family. UbiB subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00414}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein
CC kinase family. {ECO:0000256|ARBA:ARBA00009670}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00414}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGZ44675.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGFD01000040; EGZ44675.1; -; Genomic_DNA.
DR AlphaFoldDB; G4E6Q2; -.
DR STRING; 765914.ThisiDRAFT_1981; -.
DR PATRIC; fig|765914.3.peg.1967; -.
DR eggNOG; COG0661; Bacteria.
DR UniPathway; UPA00232; -.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00414}; Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00414}; Kinase {ECO:0000256|HAMAP-Rule:MF_00414};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00414};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00414};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00414};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00414};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00414}; Ubiquinone {ECO:0000313|EMBL:EGZ44675.1};
KW Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688, ECO:0000256|HAMAP-
KW Rule:MF_00414}.
FT TRANSMEM 504..524
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
FT TRANSMEM 530..553
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
FT DOMAIN 95..345
FT /note="ABC1 atypical kinase-like"
FT /evidence="ECO:0000259|Pfam:PF03109"
FT ACT_SITE 289
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
FT BINDING 132..140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
FT BINDING 154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
SQ SEQUENCE 556 AA; 63813 MW; 1626E255D0045FD4 CRC64;
MILLRPMQLL RLITINRVLI RHGLDEVIFA IHLLRPIRFL FYLAPWNWFR RVRASRGERI
RRTLEDLGPI FIKFGQMLST RRDLLPDDIA KELARLQDRV PPFPDAQAFA IIERALGKPI
SEVFLAFDKT PLASASIAQV YAAVLHSGEP VVVKVVRPDI LPVIRRDLQL MYIMAQLAER
YWSEGPRLRP VEVVAEYEKT ILDELDLMRE AANATQIKRN FSGSSILYIP TIYWDYTRRQ
VMVMERIHGV PVADMQALSA VGADLKLLSE RGVEIFFTQV FRHNFFHADM HPGNIFIDID
IPEDPTYIAV DFGIVGTLTG ADRRYLAENF HAFFNRDYRR VAELHVESGW VPADTRTEQL
ESAIRSVCEP IFQRPLKDIS FGQLLLRLFQ TARRYDMQVQ PQLVLLQKTL LNIEGLGRDL
YPDLDLWKTA KPFIERWIDE QVGLRAMIRG AKYGLPVFLE KLPQMPGLMH EIMLHEAKGR
TRRDISAPQL EALRQEIIRA QQRSSLTVLA ATLFICATLL LLFAENLPGY LGIPYAAAGM
VALAGLLLLM ALWRRG
//
