ID A0A0F7JRT9_9DEIO Unreviewed; 683 AA.
AC A0A0F7JRT9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=V-type ATP synthase subunit I {ECO:0000256|RuleBase:RU361189};
GN ORFNames=SY84_08485 {ECO:0000313|EMBL:AKH18437.1};
OS Deinococcus soli (ex Cha et al. 2016).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=1309411 {ECO:0000313|EMBL:AKH18437.1, ECO:0000313|Proteomes:UP000034024};
RN [1] {ECO:0000313|EMBL:AKH18437.1, ECO:0000313|Proteomes:UP000034024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N5 {ECO:0000313|EMBL:AKH18437.1,
RC ECO:0000313|Proteomes:UP000034024};
RA Kim M.K., Srinivasan S., Lee J.-J.;
RT "Deinococcus soli/N5/whole genome sequencing.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP011389; AKH18437.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7JRT9; -.
DR KEGG; dch:SY84_08485; -.
DR PATRIC; fig|1309411.5.peg.1732; -.
DR Proteomes; UP000034024; Chromosome.
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 Gene3D; 1.20.1460.20; -; 1.
DR Gene3D; 3.30.70.2170; -; 1.
DR Gene3D; 3.30.70.2750; -; 1.
DR InterPro; IPR002490; V-ATPase_116kDa_su.
DR InterPro; IPR040574; V_ATPase_I_N.
DR PANTHER; PTHR11629:SF63; V-TYPE PROTON ATPASE SUBUNIT A; 1.
DR PANTHER; PTHR11629; VACUOLAR PROTON ATPASES; 1.
DR Pfam; PF01496; V_ATPase_I; 1.
DR Pfam; PF18670; V_ATPase_I_N; 1.
PE 3: Inferred from homology;
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU361189};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361189};
KW Reference proteome {ECO:0000313|Proteomes:UP000034024};
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 344..375
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 476..499
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 551..568
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 588..610
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 616..642
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT DOMAIN 112..200
FT /note="V-type ATP synthase subunit I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18670"
SQ SEQUENCE 683 AA; 74835 MW; 81012496C110E83D CRC64;
MQQVVIATRK RDSEAVIAAL QDAGVLHLKP ITGGPLSTGS LAGADAQSRR EDERLLARAE
STLAELGSYR PAPASLPAAE GWADLIEQAA QPTAALARQR QDLQADLDAE SAYGDAVRAL
GRMAGSLDRS QRVSLLPFVL QATDNSGELD AALKAELADR YVLATETVGA NRVGLIATRR
SERDLARAAL GKVRLGELRL PGRFDGLPLG EAAAEMDRVA RTGTARLGEL NAERDRLAQA
HAPALYAIRD ALKDRVAIHD VRAVSARGKY SLALQGYVPE DRLAALKGAL DRFGSAVSYD
LHPVDDHHDD LVPVELKNNS YVKPFQTVMG LMTPPKYGTF DPTWVVALFF PLFFGIIMAD
IGYGLLFLWF GMWLLGKAKR NEGWDLSFFG AYVPPATLRD LGFVTNVMAA WTILWGFLTG
EFFGTFLEHF GIFYINPELL NSLWGWTGIR YPEEAEAHKT LFHLFPILFP RLETGYFSNV
ALVFALCFGI LQVLWGWAIR IQQGLKHKDP VHTWEGIALF GGVGALILMA FATKAGKDFS
AFTNFSDPRV LLMYVGFAAF VVGWLRVIKH YPLLPIELLS QGGAVVSYAR IFAVGLVSAI
LAKLCTDLGW SLYENIGFLG IIIGILLGLV LHFLVLALTL IGHVLQPLRL HMVEFLNPTG
FNADSSPRYN PLRRLSPAQG QVK
//