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ATP6_SOLM1
ID   ATP6_SOLM1              Reviewed;         238 AA.
AC   C4XQ07;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 73.
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}; OrderedLocusNames=DMR_42160;
OS   Solidesulfovibrio magneticus (strain ATCC 700980 / DSM 13731 / RS-1)
OS   (Desulfovibrio magneticus).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Solidesulfovibrio.
OX   NCBI_TaxID=573370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700980 / DSM 13731 / RS-1;
RX   PubMed=19675025; DOI=10.1101/gr.088906.108;
RA   Nakazawa H., Arakaki A., Narita-Yamada S., Yashiro I., Jinno K., Aoki N.,
RA   Tsuruyama A., Okamura Y., Tanikawa S., Fujita N., Takeyama H.,
RA   Matsunaga T.;
RT   "Whole genome sequence of Desulfovibrio magneticus strain RS-1 revealed
RT   common gene clusters in magnetotactic bacteria.";
RL   Genome Res. 19:1801-1808(2009).
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; AP010904; BAH77707.1; -; Genomic_DNA.
DR   RefSeq; WP_015862832.1; NC_012796.1.
DR   AlphaFoldDB; C4XQ07; -.
DR   SMR; C4XQ07; -.
DR   STRING; 573370.DMR_42160; -.
DR   EnsemblBacteria; BAH77707; BAH77707; DMR_42160.
DR   KEGG; dma:DMR_42160; -.
DR   eggNOG; COG0356; Bacteria.
DR   HOGENOM; CLU_041018_2_2_7; -.
DR   OMA; FFDQFMS; -.
DR   Proteomes; UP000009071; 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; IPR045082; ATP_syn_F0_a_bact/chloroplast.
DR   InterPro; IPR000568; ATP_synth_F0_asu.
DR   InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR   InterPro; IPR035908; F0_ATP_A_sf.
DR   PANTHER; PTHR42823; PTHR42823; 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..238
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_1000215143"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        190..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        211..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
SQ   SEQUENCE   238 AA;  26406 MW;  53956250F6E7B121 CRC64;
     MAGGLPHPVL LVDEAAKSVG LYKLNDVFHA QVIDSNVIYA WFAMVLLIIL GTLATRKLAM
     VPSGLQNFFE VVVGGLESFV VENIGEKGRK VYPFLCALFL FIITGNLIGL VPGLDSPTNN
     VNTNAAMALT VFAYYNFWGI RMWGAGYIKH FMGPFWWLVP LMLPIEIISH LARPLSLTLR
     LFGNIRGEEI VLVLLFALAP VVGTFPMYFL FSLADCIQAF VFFMLAMIYL KGSLDHAH
 
 
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