Y1806_AQUAE
ID Y1806_AQUAE Reviewed; 206 AA.
AC O67672;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Uncharacterized lipoprotein aq_1806;
DE Flags: Precursor;
GN OrderedLocusNames=aq_1806;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
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DR EMBL; AE000657; AAC07642.1; -; Genomic_DNA.
DR PIR; F70455; F70455.
DR RefSeq; NP_214238.1; NC_000918.1.
DR RefSeq; WP_010881175.1; NC_000918.1.
DR AlphaFoldDB; O67672; -.
DR SMR; O67672; -.
DR STRING; 224324.aq_1806; -.
DR EnsemblBacteria; AAC07642; AAC07642; aq_1806.
DR KEGG; aae:aq_1806; -.
DR eggNOG; COG2010; Bacteria.
DR HOGENOM; CLU_098286_0_0_0; -.
DR OrthoDB; 1853490at2; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.760.10; -; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR030999; Thiosulf_SoxX.
DR InterPro; IPR016823; Thiosulf_SoxX_II.
DR PIRSF; PIRSF024608; UCP024608; 1.
DR SUPFAM; SSF46626; SSF46626; 1.
DR TIGRFAMs; TIGR04485; thiosulf_SoxX; 1.
DR PROSITE; PS51007; CYTC; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell membrane; Coiled coil; Electron transport; Heme; Iron; Lipoprotein;
KW Membrane; Metal-binding; Palmitate; Reference proteome; Signal; Transport.
FT SIGNAL 1..17
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 18..206
FT /note="Uncharacterized lipoprotein aq_1806"
FT /id="PRO_0000006606"
FT DOMAIN 97..201
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT COILED 21..58
FT /evidence="ECO:0000255"
FT BINDING 127
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 130
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 131
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT LIPID 18
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 18
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 206 AA; 22717 MW; 6218890797221A53 CRC64;
MKGKILFALF LSAGVIACQP ASQAAKQQEV KVAKAETKTK KKESKAEKFR KALAAQDKWQ
KACSNPVQIA PEGVDVAQFI KEMKATIKYP EDGNVVGDWR KGESLALLKK EYKALYGKKG
GSKKGNCYAC HCGDPRIIAC GNIGPSLRGY GNKGIDPKMT YERIYNPWSQ VPCSTMFRFG
YHGLLTPEEI ADIVAYLHDP ESPINK
