ID A9NGV8_ACHLI Unreviewed; 635 AA.
AC A9NGV8;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=V-type ATP synthase subunit I {ECO:0000256|RuleBase:RU361189};
GN Name=ntpI1 {ECO:0000313|EMBL:ABX81588.1};
GN OrderedLocusNames=ACL_0978 {ECO:0000313|EMBL:ABX81588.1};
OS Acholeplasma laidlawii (strain PG-8A).
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Acholeplasma.
OX NCBI_TaxID=441768 {ECO:0000313|EMBL:ABX81588.1, ECO:0000313|Proteomes:UP000008558};
RN [1] {ECO:0000313|EMBL:ABX81588.1, ECO:0000313|Proteomes:UP000008558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG-8A {ECO:0000313|EMBL:ABX81588.1,
RC ECO:0000313|Proteomes:UP000008558};
RX PubMed=21784942; DOI=10.1128/JB.05059-11;
RA Lazarev V.N., Levitskii S.A., Basovskii Y.I., Chukin M.M., Akopian T.A.,
RA Vereshchagin V.V., Kostrjukova E.S., Kovaleva G.Y., Kazanov M.D.,
RA Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S., Demina I.A.,
RA Serebryakova M.V., Galyamina M.A., Vtyurin N.N., Rogov S.I., Alexeev D.G.,
RA Ladygina V.G., Govorun V.M.;
RT "Complete genome and proteome of Acholeplasma laidlawii.";
RL J. Bacteriol. 193:4943-4953(2011).
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; CP000896; ABX81588.1; -; Genomic_DNA.
DR AlphaFoldDB; A9NGV8; -.
DR STRING; 441768.ACL_0978; -.
DR KEGG; acl:ACL_0978; -.
DR eggNOG; COG1269; Bacteria.
DR HOGENOM; CLU_025558_1_0_14; -.
DR Proteomes; UP000008558; Chromosome.
DR GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:ABX81588.1};
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:UP000008558};
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 337..364
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 376..402
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 455..474
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 480..500
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 554..574
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
SQ SEQUENCE 635 AA; 71823 MW; 82AF69896971CDEC CRC64;
MIVSMQKVKL IFLESDKEQI LNELQMHALF MPDKKHFKSV TPSEDLIRVS KAIEIIERYL
KKSTGNNAIV TKSEFELLDQ HSLELAANIL DLQNTYYKLQ ETQKSLKEKY EELLPYKNLS
VSQSRIETLR FTQVVLGFIQ KEKYDAFKGH MDTLGAYVDI LSSDDNYHYV SILIDKDQSD
RLEDLLESMD FNIEPNRNYD KTNMEVITDL NSELESIEKE MKETEQFFID SSKDLGGLKL
LHDQLLSKES KLQIELLSTE TTVYVEGWVR GDQVEDIKTI LNDKNFVFEL EARDALSDES
VPTALKNNGF VKPYEYITNQ FSTPSASEVD PNPSMSFWYW LIFGIMMGDI GYGLVMIVAF
GLLLKFGKLR GATKDLVKIF CYSGVTSIGA GILFGSFFGA TIFTPLLDPI NDPVPMLIIS
LILGVVHIVH GLILKLINSY RQKDILGGLN DAGSWIFILV GLSLFITATF IPLESLIQNI
LLYTSYVLMG LGVLIIILLN GREQKSIPGK IVSAIAGLYN STSYLSDILS YSRILALSLS
TAVIAYTMNL LGEMVWGSIP VLGILLGIII YLIGHVFNFI MGMLSAYVHA GRLQYLEFYG
KFFEGGGYLF EPFSLQLKYV YQVNLKENKE INKEN
//
