ATPL_METJA
ID ATPL_METJA Reviewed; 220 AA.
AC Q57674;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Probable ATPase proteolipid chain;
GN OrderedLocusNames=MJ0221;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000305}.
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DR EMBL; L77117; AAB98207.1; -; Genomic_DNA.
DR PIR; F64327; F64327.
DR RefSeq; WP_010869717.1; NC_000909.1.
DR AlphaFoldDB; Q57674; -.
DR SMR; Q57674; -.
DR STRING; 243232.MJ_0221; -.
DR EnsemblBacteria; AAB98207; AAB98207; MJ_0221.
DR GeneID; 1451071; -.
DR KEGG; mja:MJ_0221; -.
DR eggNOG; arCOG02455; Archaea.
DR HOGENOM; CLU_1237912_0_0_2; -.
DR InParanoid; Q57674; -.
DR OMA; NFIQLGA; -.
DR OrthoDB; 116293at2157; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR Gene3D; 1.20.120.610; -; 1.
DR Gene3D; 1.20.20.10; -; 1.
DR InterPro; IPR038662; ATP_synth_F0_csu_sf.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR000245; ATPase_proteolipid_csu.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR Pfam; PF00137; ATP-synt_C; 3.
DR PRINTS; PR00122; VACATPASE.
DR SUPFAM; SSF81333; SSF81333; 3.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Hydrogen ion transport; Hydrolase;
KW Ion transport; Lipid-binding; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..220
FT /note="Probable ATPase proteolipid chain"
FT /id="PRO_0000071731"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 220 AA; 21332 MW; 72DA35D2448BEAE6 CRC64;
MVDPLILGAV GAGLAVGIAG LGSGIGAGIT GASGAGVVAE DPNKFGTAIV FQALPQTQGL
YGFLVAILIL FVFKTVSPWA MFAAGLAAGL AGLSAIGQGI AASAGLGAVA EDNSIFGKAM
VFSVLPETQA IYGLLIAILL LVGVFKGNAG AETVAALGAG FAVGFAGLSG IGQGITAAGA
IGATARDPDA MGKGLVLAVM PETFAIFGLL IAILIMLMIK