VATI_PYRHO
ID VATI_PYRHO Reviewed; 659 AA.
AC O57721;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=V-type ATP synthase subunit I;
DE AltName: Full=V-ATPase subunit I;
GN Name=atpI; OrderedLocusNames=PH1981;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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; BA000001; BAA31108.1; -; Genomic_DNA.
DR PIR; E71214; E71214.
DR RefSeq; WP_010886044.1; NC_000961.1.
DR AlphaFoldDB; O57721; -.
DR SMR; O57721; -.
DR STRING; 70601.3258425; -.
DR PRIDE; O57721; -.
DR EnsemblBacteria; BAA31108; BAA31108; BAA31108.
DR GeneID; 1442826; -.
DR KEGG; pho:PH1981; -.
DR eggNOG; arCOG04138; Archaea.
DR OMA; MAVNIMA; -.
DR OrthoDB; 14889at2157; -.
DR Proteomes; UP000000752; 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; 2.
DR Pfam; PF01496; V_ATPase_I; 2.
PE 3: Inferred from homology;
KW Cell membrane; Hydrogen ion transport; Ion transport; Membrane;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..659
FT /note="V-type ATP synthase subunit I"
FT /id="PRO_0000119233"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 489..509
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 518..538
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 542..562
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 568..588
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 590..610
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 659 AA; 74308 MW; EE4B1AEEB97FCA33 CRC64;
MFKPEKIVKI EVITLTRFRD TLLTYLHEIG VAQLEEVPIK EVQRDTPNEF YRKATSYSIT
LSRLVDTLKQ YLPPKKGGFK EFMFPQEKPK KKYKYKGIEA LIKDVETFLE RVEPEIRSLE
SEVSRINNEI SSLEDTLESL QILSNLNVEV EYLRGGSFLN VDVGLVDREK AEPLIKEISD
VVEGRVHIVR KDIGARTLLV VVSLREDSSK VSSVLAKYGF EKIEVPEGKG LPRDLIPIYT
EKIKEKEKEL EEVKSRGRKV AERYYDELVF YKELMDNERE KGNYLSYLVR TEMTFGLLAW
VPEKDVEKVV EGIKKITGGV AYINISEPSK EEIDNVPVKL KNPEFLSHFE MLTEMYGVPK
YNEIDPTPIM AFTYSFFFGF MLTDFVYGLL LGIISALLVK GHSKLKDGTW KFAKIMLWSS
VFTMTLGILF GSYCGNALDM AGIKVPRILD PMEQALTVLM IALAIGLAHL FTGYLLGFIV
RWKNGDKKGA IFEQLSWLLI IIGITLFALS SRLGVPDLIV KGIFGIGLIL FMIGEVLANK
GMAVLLVISD FFGFVGNWLS YARLMALALA TSGIALVINI LVEMIWGIKI ASVPLGALIG
ILVLIGGHIF STAINALGAF VHALRLHYVE FFGTFYSGEG RKFEPFAAKR EVSELEIET