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ATP6_EHRRW
ID   ATP6_EHRRW              Reviewed;         243 AA.
AC   Q5HA45; Q5FDW7;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=ATP synthase subunit a {ECO:0000255|HAMAP-Rule:MF_01393};
DE   AltName: Full=ATP synthase F0 sector subunit a {ECO:0000255|HAMAP-Rule:MF_01393};
DE   AltName: Full=F-ATPase subunit 6 {ECO:0000255|HAMAP-Rule:MF_01393};
GN   Name=atpB {ECO:0000255|HAMAP-Rule:MF_01393};
GN   OrderedLocusNames=Erum8360, ERWE_CDS_08870;
OS   Ehrlichia ruminantium (strain Welgevonden).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=254945;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Welgevonden;
RX   PubMed=15637156; DOI=10.1073/pnas.0406633102;
RA   Collins N.E., Liebenberg J., de Villiers E.P., Brayton K.A., Louw E.,
RA   Pretorius A., Faber F.E., van Heerden H., Josemans A., van Kleef M.,
RA   Steyn H.C., van Strijp M.F., Zweygarth E., Jongejan F., Maillard J.C.,
RA   Berthier D., Botha M., Joubert F., Corton C.H., Thomson N.R., Allsopp M.T.,
RA   Allsopp B.A.;
RT   "The genome of the heartwater agent Ehrlichia ruminantium contains multiple
RT   tandem repeats of actively variable copy number.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:838-843(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Welgevonden;
RX   PubMed=16547041; DOI=10.1128/jb.188.7.2533-2542.2006;
RA   Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
RA   Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.;
RT   "Comparative genomic analysis of three strains of Ehrlichia ruminantium
RT   reveals an active process of genome size plasticity.";
RL   J. Bacteriol. 188:2533-2542(2006).
CC   -!- FUNCTION: Key component of the proton channel; it plays a direct role
CC       in the translocation of protons across the membrane.
CC       {ECO:0000255|HAMAP-Rule:MF_01393}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC       subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an
CC       alternating ring which encloses part of the gamma chain. CF(1) is
CC       attached to CF(0) by a central stalk formed by the gamma and epsilon
CC       chains, while a peripheral stalk is formed by the delta and b chains.
CC       {ECO:0000255|HAMAP-Rule:MF_01393}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01393}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01393}.
CC   -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000255|HAMAP-
CC       Rule:MF_01393}.
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DR   EMBL; CR767821; CAH58571.1; -; Genomic_DNA.
DR   EMBL; CR925678; CAI27381.1; -; Genomic_DNA.
DR   RefSeq; WP_011155515.1; NC_006832.1.
DR   AlphaFoldDB; Q5HA45; -.
DR   SMR; Q5HA45; -.
DR   STRING; 254945.Erum8360; -.
DR   EnsemblBacteria; CAI27381; CAI27381; ERWE_CDS_08870.
DR   GeneID; 56785613; -.
DR   KEGG; eru:Erum8360; -.
DR   KEGG; erw:ERWE_CDS_08870; -.
DR   eggNOG; COG0356; Bacteria.
DR   HOGENOM; CLU_041018_0_2_5; -.
DR   OMA; FFDQFMS; -.
DR   BioCyc; ERUM254945:ERUM_RS04520-MON; -.
DR   Proteomes; UP000001021; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.120.220; -; 1.
DR   HAMAP; MF_01393; ATP_synth_a_bact; 1.
DR   InterPro; IPR000568; ATP_synth_F0_asu.
DR   InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR   InterPro; IPR045083; ATP_synth_F0_asu_bact/mt.
DR   InterPro; IPR035908; F0_ATP_A_sf.
DR   PANTHER; PTHR11410; PTHR11410; 1.
DR   Pfam; PF00119; ATP-synt_A; 1.
DR   PRINTS; PR00123; ATPASEA.
DR   SUPFAM; SSF81336; SSF81336; 1.
DR   TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1.
DR   PROSITE; PS00449; ATPASE_A; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Cell inner membrane; Cell membrane; CF(0);
KW   Hydrogen ion transport; Ion transport; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..243
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_0000362292"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        177..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        200..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        221..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
SQ   SEQUENCE   243 AA;  27030 MW;  C5C62A37A1DCD09C CRC64;
     MSANPLDQFR ISTIFKLPDI GEYNIDFTNA SLFMVLSTFL ISLSCYVGLR KESVIPNPLQ
     SIIEIIYDFI VSTIESNVGK EGLQYVPLVF TIFTFILVCN LLGILPLGFT VTSHIAVTFA
     ISMIVFISVT FIGFKHQGTH FLHILLPQGT PMWLAPMMVL IELFAYCARP VSLSIRLAAN
     MIAGHTIIKV IAGFVINMNI FLTPLPIAFI IILIGFEIFV AILQAYIFTV LTCVYLSDAV
     NKH
 
 
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