ID A0A1M6MIV3_9BURK Unreviewed; 525 AA.
AC A0A1M6MIV3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=SAMN05192548_1007186 {ECO:0000313|EMBL:SHJ83324.1};
OS Paraburkholderia terricola.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=169427 {ECO:0000313|EMBL:SHJ83324.1, ECO:0000313|Proteomes:UP000184395};
RN [1] {ECO:0000313|EMBL:SHJ83324.1, ECO:0000313|Proteomes:UP000184395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 20594 {ECO:0000313|EMBL:SHJ83324.1,
RC ECO:0000313|Proteomes:UP000184395};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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 Single-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}.
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DR EMBL; FRAB01000007; SHJ83324.1; -; Genomic_DNA.
DR RefSeq; WP_073428284.1; NZ_JAVDRP010000002.1.
DR AlphaFoldDB; A0A1M6MIV3; -.
DR STRING; 169427.SAMN05192548_1007186; -.
DR KEGG; pts:CUJ90_02115; -.
DR OrthoDB; 9795390at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000184395; Unassembled WGS sequence.
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};
KW Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688, ECO:0000256|HAMAP-
KW Rule:MF_00414}.
FT TRANSMEM 501..523
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
FT DOMAIN 87..340
FT /note="ABC1 atypical kinase-like"
FT /evidence="ECO:0000259|Pfam:PF03109"
FT ACT_SITE 285
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
FT BINDING 124..132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
FT BINDING 150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
SQ SEQUENCE 525 AA; 59710 MW; 6A5EC734FEE28AB0 CRC64;
MRFLRFLKIF FTVIRFGLDE MMLGRINDRR VRLLLRITTI GRKFDAPPGV RLRLALESLG
PIFVKFGQVL STRRDLLPVD IANELAKLQD QVPPFDSTVA IGLVEKSLGA PVDVLFDDFE
RVPVASASIA QVHFAKVKAG QHAGKAVAVK VLRPNMLPVI DSDLALLRDI AVWAERLWAD
GKRLKPREVV AEFDKYLHDE LDLMREAANG SQLRRNFAGL DLLLVPEMYW EFCTPTVLVM
ERMVGVPISQ VETLRGAGVD IPKLAREGVE IFFTQVFRDG FFHADMHPGN IQVSLDPVHF
GRYIALDFGI IGALSDFDKN YLAQNFLAFF KRDYHRVATL HLESGWVPPT TRVEELESAI
RAVCEPYFDR ALKDISLGQV LMRLFSTSRR FNVEIQPQLV LLQKTMLNVE GLGRSLDPEL
DLWKTAKPYL ERWMNEQIGL RGWYERLKIE APQWSKTLPQ LPRLIHHVLA ERHDHGRGMN
DDMIRQILLE QKRTNRLLQG LLLFGVAVGV GAVLARAFLA FAYGG
//
