ID M5TS64_9BACT Unreviewed; 604 AA.
AC M5TS64;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 04-NOV-2026, entry version 40.
DE SubName: Full=Ubiquinone biosynthesis protein AarF {ECO:0000313|EMBL:EMI52000.1};
GN ORFNames=RSSM_06565 {ECO:0000313|EMBL:EMI52000.1};
OS Aporhodopirellula sallentina SM41.
OC Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia; Pirellulales;
OC Pirellulaceae; Aporhodopirellula.
OX NCBI_TaxID=1263870 {ECO:0000313|EMBL:EMI52000.1, ECO:0000313|Proteomes:UP000011885};
RN [1] {ECO:0000313|EMBL:EMI52000.1, ECO:0000313|Proteomes:UP000011885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM41 {ECO:0000313|EMBL:EMI52000.1,
RC ECO:0000313|Proteomes:UP000011885};
RX PubMed=23273849;
RA Wegner C.E., Richter-Heitmann T., Klindworth A., Klockow C., Richter M.,
RA Achstetter T., Glockner F.O., Harder J.;
RT "Expression of sulfatases in Rhodopirellula baltica and the diversity of
RT sulfatases in the genus Rhodopirellula.";
RL Mar. Genomics 0:0-0(2013).
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis [regulation].
CC {ECO:0000256|ARBA:ARBA00005020}.
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:EMI52000.1}.
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DR EMBL; ANOH01000458; EMI52000.1; -; Genomic_DNA.
DR AlphaFoldDB; M5TS64; -.
DR PATRIC; fig|1263870.3.peg.6964; -.
DR Proteomes; UP000011885; Unassembled WGS sequence.
DR CDD; cd05121; ABC1_ADCK3-like; 1.
DR InterPro; IPR062901; ABC1_C.
DR InterPro; IPR004147; ABC1_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR050154; UbiB_kinase-like.
DR PANTHER; PTHR10566; CHAPERONE-ACTIVITY OF BC1 COMPLEX CABC1 -RELATED; 1.
DR PANTHER; PTHR10566:SF113; PROTEIN ACTIVITY OF BC1 COMPLEX KINASE 7, CHLOROPLASTIC; 1.
DR Pfam; PF03109; ABC1; 1.
DR Pfam; PF30649; ABC1_C; 1.
DR Pfam; PF27536; UbiB_helical; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000011885};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubiquinone {ECO:0000313|EMBL:EMI52000.1}.
FT TRANSMEM 539..558
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 578..599
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 98..385
FT /note="ABC1 atypical kinase-like"
FT /evidence="ECO:0000259|Pfam:PF03109"
FT DOMAIN 531..599
FT /note="ABC1/UbiB kinase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF30649"
FT REGION 260..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 604 AA; 67772 MW; 3FB47A42FEAF8E0F CRC64;
MMKLTSIPSL YRNLRRGREI LLVLRRYGLA DWLSRSQSLP FRNWIKDRSG VPLTQYSRVE
RIRMAITELG PTFIKVGQVL ASRPDLVGIE LADELKRLRG RVEPDTAEQV RATLRSELGD
DFEKNFSSIC YTPLATASIG QVHRAVLLDG SRVVLKVQRS GIDRLMRQDI EVLEGLAQLA
ARVDTIAVWG PREMVRQLRP MVLHELDFNR ERSSLKQFAD ALAPEQAEVA VPAVVDHLCT
RRVLVMEEMI GTPLASIFSH SESARKNESE SLTAASAEKT AGEDRSPNGD NHRVSPDDSE
VRIEVTKEKL PPDIGARLAK VYLKMVFEDG FFHADPHPGN LIFLDDKRLG ILDFGMTGRI
DETLRESIEE MLVAINSGDR RRLTRLIRGV GNPRLDLDQA ALEIDVADFV DTYGRQSLDR
FDLSGALNEL TEILHRHGIT LPNQSALLLK MLISLEGTLR ELGVGFDSLD IVRTYLRKVM
FRRLTPTRRL RQARRIYLEN EAFLEEAPEQ LLAVLNQTRL GQLQIRLDPK RITPSVNRLV
LGLMASAVFL GSSLLLAYEV PPLLFPDTSV AGIERLSLLG LLGLIASTSV MTGLCITILS
NNRD
//
