ID A0A2Z3JBB4_9DEIO Unreviewed; 684 AA.
AC A0A2Z3JBB4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=V-type ATP synthase subunit I {ECO:0000256|RuleBase:RU361189};
GN ORFNames=DKM44_03685 {ECO:0000313|EMBL:AWN22447.1};
OS Deinococcus irradiatisoli.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=2202254 {ECO:0000313|EMBL:AWN22447.1, ECO:0000313|Proteomes:UP000245368};
RN [1] {ECO:0000313|EMBL:AWN22447.1, ECO:0000313|Proteomes:UP000245368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17bor-2 {ECO:0000313|EMBL:AWN22447.1,
RC ECO:0000313|Proteomes:UP000245368};
RA Srinivasan S.;
RT "Complete Genome Sequence of Deinococcus sp. strain 17bor-2.";
RL Submitted (MAY-2018) 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; CP029494; AWN22447.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z3JBB4; -.
DR KEGG; dez:DKM44_03685; -.
DR OrthoDB; 9803814at2; -.
DR Proteomes; UP000245368; 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:UP000245368};
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 354..382
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 478..498
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 510..529
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 549..571
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 583..602
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 614..639
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT DOMAIN 116..206
FT /note="V-type ATP synthase subunit I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18670"
SQ SEQUENCE 684 AA; 74711 MW; B2693968890728AB CRC64;
MINPMQQVVI ATRKRESRAV IEALQDAGAL HLVPVQGAGV LSAGPLSGED AEFRRESERL
LARTETTLTE LGAVRRAAAP LPAEEQWPEL LEEVARPAAE LAKRRQALDG DLDVWRTYGP
AVKALSDLSG GLDRSRRVSL VPFIYQKPEE LAALQAALQA SLEGRFELAT RPLSGSDFVG
AVATLTIDRD AARAALGKAR LGELRLPGRF DGQPISEVAR ELGRIEREGV AQRDALERER
VSLADRFGPT LFAIRDALSD QVAIHDVQGM SARGKYSLVM QGFVPDDRVA GLKTALDRFG
NAVSYELHPV DSHHTAHVPV ELKNSSYSKN FELILGMLPL PRYGNFDPTG IISFFFPLFF
GFIIADIGYG LLFFILGTWF ATKARRGEGF NLAAMNSYLS PGVMGKLGVI IRTMSTWAIF
WGFLTGEFFG NLAEHLHLFY FNHAWMQSLW GITVPGEQES GLLPIVFPRL QPWFTNTALI
STLLVGILMV IWGWLIRVQL ASRHGDKNHL WEAIGMIGGL VGLVSLGFLS QGGNQLVNGS
IYTDFSSPLL IVMYLGFAVF LVGMVMSKVF LMIIEILSQG GNIISFARLF AVGVAGAILA
NLATDLGWGM YERIGILGIL IGIVLALLVH AFALAITIIG HVLQPIRLHF VEFLTPTGYH
NESGVAYNPL RRLSPAASTA ASKK
//
