ID A0A1M3DCT9_9SPHN Unreviewed; 512 AA.
AC A0A1M3DCT9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=2-polyprenylphenol 6-hydroxylase {ECO:0000313|EMBL:OJV32073.1};
GN ORFNames=BGO24_14500 {ECO:0000313|EMBL:OJV32073.1};
OS Sphingomonas sp. 67-36.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1895849 {ECO:0000313|EMBL:OJV32073.1, ECO:0000313|Proteomes:UP000183964};
RN [1] {ECO:0000313|EMBL:OJV32073.1, ECO:0000313|Proteomes:UP000183964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=67-36 {ECO:0000313|EMBL:OJV32073.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis [regulation].
CC {ECO:0000256|ARBA:ARBA00005020}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein
CC kinase family. {ECO:0000256|ARBA:ARBA00009670}.
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:OJV32073.1}.
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DR EMBL; MKSU01000014; OJV32073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3DCT9; -.
DR STRING; 1895849.BGO24_14500; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000183964; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd13972; 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};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688}.
FT TRANSMEM 488..511
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 91..337
FT /note="ABC1 atypical kinase-like"
FT /evidence="ECO:0000259|Pfam:PF03109"
SQ SEQUENCE 512 AA; 56316 MW; 68ACA78F506424CA CRC64;
MTSPIVHSWR LLKWGRILAR HGALRGIERD PNTPPRLRRL LRIARFGART PNVPRYADAF
QAIGPAAIKL GQTLATRPDL VGEAAAADLL RLQDALPPVP FAEIRPQLQA SFGRPLDHLF
AHIDEVPVGA ASIAQVHRAV TTDGREVAVK VLRPGVEEEF ARAIETYEWA AAQAEPMGGE
IARLQPRLVI ETFKRWTARE LDLRREAASA SELAEGMTAE PGYIVPKVDW QRTTGKVLTI
EWIDGIKLSD RAALVAQGYD LPALARTLVH AFLRQAIAEG FFHADMHQGN LFAVPGNRIV
AIDFGIMGRI DRRARVWLAE ILYGLITGNY RRVAEIHFEA GYVPPHHNVA EFATALRAVG
EPMRGLPVKE MSIGMMLDGL FSITRDFDMA TQPHLLLLQK TMVMVEGVAT SLDPDINMWD
TAGPVVEEWI RTELGPEAAI ADRLVADFRT LARLPDLVRR IEERFPAPGG APPTPPLREI
EVVRIGGGWR YAAVALIAAL AGAGAALAAI WL
//
