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Database: UniProt
Entry: M0A867_9EURY
LinkDB: M0A867_9EURY
Original site: M0A867_9EURY 
ID   M0A867_9EURY            Unreviewed;       766 AA.
AC   M0A867;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=V-type ATP synthase subunit I {ECO:0000256|ARBA:ARBA00020764, ECO:0000256|RuleBase:RU361189};
GN   ORFNames=C484_06624 {ECO:0000313|EMBL:ELY94077.1};
OS   Natrialba taiwanensis DSM 12281.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrialba.
OX   NCBI_TaxID=1230458 {ECO:0000313|EMBL:ELY94077.1, ECO:0000313|Proteomes:UP000011648};
RN   [1] {ECO:0000313|EMBL:ELY94077.1, ECO:0000313|Proteomes:UP000011648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12281 {ECO:0000313|EMBL:ELY94077.1,
RC   ECO:0000313|Proteomes:UP000011648};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00009904, ECO:0000256|RuleBase:RU361189}.
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:ELY94077.1}.
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DR   EMBL; AOIL01000018; ELY94077.1; -; Genomic_DNA.
DR   RefSeq; WP_006825143.1; NZ_AOIL01000018.1.
DR   AlphaFoldDB; M0A867; -.
DR   STRING; 1230458.C484_06624; -.
DR   PATRIC; fig|1230458.4.peg.1342; -.
DR   OrthoDB; 85892at2157; -.
DR   Proteomes; UP000011648; Unassembled WGS sequence.
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:SF63; V-TYPE PROTON ATPASE SUBUNIT A; 1.
DR   PANTHER; PTHR11629; VACUOLAR PROTON ATPASES; 1.
DR   Pfam; PF01496; V_ATPase_I; 2.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU361189};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361189};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU361189};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU361189};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM        409..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        447..469
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        506..528
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        540..559
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        603..622
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        643..665
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        704..725
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   REGION          317..385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          79..113
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          223..250
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        317..335
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   766 AA;  83471 MW;  C7AA5E90D3FFE7ED CRC64;
     MSKVSVTGAK GIMPTVIETI HELNLVHLSD YDGSWEGFDN GNPIEGADDA SEKLVTVRAL
     ESTLDLADAE TPAPRGTLAD NWEQRLEEVR TRVNELDDQR TEIREELRQV EDRIDRVSPF
     AELGIDLDLL SGYETVDILV GEGSPGEIEA ELDAAEDIRA YETFTSGDVI AIVAAPTDAV
     EAAVDESESG SEDDGNVIDD ALVGIEFTRY DVPDTDQSPS GYVAELEERK TDLESRLTEI
     DDELERIERE DGQFLLQLEE ELTIEVQRAE APLQFATSNR AFIAEGWVPS DEFGRLTTAL
     RNAVGDSLEI EELERASYDR HGAHSHTEEI QKGTPEGDAD APAQTDADAT ADDEAADGEK
     QTAVTDGGSA VTMGDEPPTI QDNPSAAKPF EVLVQAVNRP KYSELDPTIF LFLTFPAFFG
     FMIGDVGYGL LYVAIGAYMA TQFDSKGITS LGGVAIWAGL FTILFGFIYG EIFGLHVLGE
     VLWHDTLHVD LLPLNKGLEP AAADFALGWM VVSVIAGIVH LNIGYILDFY ENMSHGVKDA
     VMHSGSWLLM LNGIWIWIFS AQARGSKPDF LFNTFASDGP FPIGFTGFPE WGLVTIPLGV
     TEFLLTAPLL VFLIGFVMLL VTDTVEAVEA LDVIVNVFSY TRMGAVLLAK AGMAFVVNLL
     FFGAYRDPDG AFHFLRTHEP SYVAEHYGDG AEVIFNGLMH SGTAALVGGL VILVVGHLVV
     LALGVTSAGL QAVRLEYVEF FNKFYEGGGA NYEPFGHDRN DTEDHY
//
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