ID C1CXT8_DEIDV Unreviewed; 687 AA.
AC C1CXT8;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=V-type ATP synthase subunit I {ECO:0000256|RuleBase:RU361189};
GN Name=atpI {ECO:0000313|EMBL:ACO44894.1};
GN OrderedLocusNames=Deide_00940 {ECO:0000313|EMBL:ACO44894.1};
OS Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO44894.1, ECO:0000313|Proteomes:UP000002208};
RN [1] {ECO:0000313|EMBL:ACO44894.1, ECO:0000313|Proteomes:UP000002208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115
RC {ECO:0000313|Proteomes:UP000002208};
RX PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT bacterium Deinococcus deserti.";
RL PLoS Genet. 5:E1000434-E1000434(2009).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001114; ACO44894.1; -; Genomic_DNA.
DR RefSeq; WP_012692017.1; NC_012526.1.
DR AlphaFoldDB; C1CXT8; -.
DR STRING; 546414.Deide_00940; -.
DR PaxDb; 546414-Deide_00940; -.
DR KEGG; ddr:Deide_00940; -.
DR eggNOG; COG1269; Bacteria.
DR HOGENOM; CLU_025558_2_1_0; -.
DR OrthoDB; 9803814at2; -.
DR Proteomes; UP000002208; 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:UP000002208};
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 348..379
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 400..422
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 477..500
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 552..569
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 589..611
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 617..643
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT DOMAIN 115..204
FT /note="V-type ATP synthase subunit I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18670"
FT REGION 668..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 687 AA; 75537 MW; 93F272330CD88829 CRC64;
MINPMQQVVI ATRKRDSESV IAALQDAGVL HLKPITGGPL NTGTLAGQDA QHRREDERLL
ARVDSTIAEL GAYRPAPTSL PAQSEWAEVV EAAAGPVSTL ARERQELQAD LDTERAYGDV
VRALARMVGG LSRSRRVALV PFLLSPADNA SELDAALREA LADRYEMAME SVGANRVGVI
ATLRGERDAA RAALSRVRLG ELRLPGRFDQ LPLADAAAEL DQIARTGADR QRQLNDRRDR
LAQTHGPVLY AVRDALKDRV AVHDVRAVSA RGKYSLAMQG YVPVDRVPAL QAALGKFGDA
VSYELHPVDE HHDDAVPVQL KNNGYVKPFQ TVMGLMSLPK YGSFDPTWVV AVFFPLFFGI
IIADIGYGLL FLLFGMWLLG KARRNEGWDL SFFGAYVPPA TLKDLGFVTN VMAAWSILWG
VLTGEFFGTL LEHMHFFYIN PDLLNNLWGW TGIRYEDHGG KHYGLIPIVF PRLETSYFSN
VALVFALLFG ILQVLWGWAI RIQQGIKHRD SAHTWEGIAL FGGVFGLVMM AFATRAGKDF
GAFGNFADPR VLLMYLGFAA FIIGYLRVIK QFPMLPIELL SQGGAVMSYS RIFAVGLVSA
ILAKLCTDVG WSMYERIGFI GILLGIILGA VLHFFVLALT LIGHIVQPLR LHMVEFLNPT
GFNNETSPAY NPLRRLSPAA NSGGQVK
//
