VATI_AERPE
ID VATI_AERPE Reviewed; 685 AA.
AC Q9YEA0;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=V-type ATP synthase subunit I;
DE AltName: Full=V-ATPase subunit I;
GN Name=atpI; OrderedLocusNames=APE_0673.1;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; BA000002; BAA79646.2; -; Genomic_DNA.
DR PIR; F72655; F72655.
DR AlphaFoldDB; Q9YEA0; -.
DR SMR; Q9YEA0; -.
DR STRING; 272557.APE_0673.1; -.
DR PRIDE; Q9YEA0; -.
DR EnsemblBacteria; BAA79646; BAA79646; APE_0673.1.
DR KEGG; ape:APE_0673.1; -.
DR eggNOG; arCOG04138; Archaea.
DR Proteomes; UP000002518; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR InterPro; IPR002490; V-ATPase_116kDa_su.
DR PANTHER; PTHR11629; PTHR11629; 1.
DR Pfam; PF01496; V_ATPase_I; 2.
PE 3: Inferred from homology;
KW Cell membrane; Hydrogen ion transport; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..685
FT /note="V-type ATP synthase subunit I"
FT /id="PRO_0000119226"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..414
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 538..558
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 604..624
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 626..646
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 685 AA; 75021 MW; 871DDDACD43E4C90 CRC64;
MLLPRMLEEV VLAVPARDYD RVVAGLAVEG IFHVDSPPQG VKGEVDRSYR ALLTQASERS
SRIRQYFDLA GVEPYRVSGV EIEVGGWGES WKRYLEKYSG VEKFYSGLLE EYSEAEARLK
ELLDIEARIA PVAHLDVDIA RLYRSGAFDF AVYYGSYSEG LESRVGEIVS RVGGLAAVEA
SGGSVVVAVA VPKGALSKIS PEILRLNLSI YTPPEGVPGS PREAMEYIRG EKARLGRRLV
SIQEMASERL GELAEFYTVV TAFENIFKFL VSTLRRGETR IVRGFVDVRD SGRLRSIVDR
MTRGSYVLLS LGVRRGGEAP IPSKVDLPQF LKPFSRVVEL YGYPEPNEIV PTVFLAITLP
LTFALMFPDA GQGLLVLLFS LFYLRRVSRD WAYVIAVMGG ASVVSGLLAG EVFGPLVSKM
LGLPELWYRL GLETPPYAMP TYAIDHGEEE LVPVLVYRAL NVSLFMGAFM LSFGTFLGVV
NGVIKRDWVG LVESRLPRFL LFASITGPFL VYMDAGEAGS VLRQALLELG GDSIAAKLVL
AGSVLGLAWM LLAGPIIYML EGHSPLAGLA NSFLEAYESL LMLVGNIPSF LRIMALALAH
SSLMFVIYYL TVMIMQGGIL ADVVGALLYV GGNLAVAAME GLLAFAHASR LHFYEWFSKF
YSGTGVPYTP IKVEGVRIKI AGQTF