ATP6_MAGMM
ID ATP6_MAGMM Reviewed; 259 AA.
AC A0LDW6;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 25-MAY-2022, entry version 82.
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=Mmc1_3674;
OS Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Magnetococcales;
OC Magnetococcaceae; Magnetococcus.
OX NCBI_TaxID=156889;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1;
RX PubMed=19465526; DOI=10.1128/aem.02874-08;
RA Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT coccus strain MC-1.";
RL Appl. Environ. Microbiol. 75:4835-4852(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK46159.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000471; ABK46159.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A0LDW6; -.
DR SMR; A0LDW6; -.
DR STRING; 156889.Mmc1_3674; -.
DR EnsemblBacteria; ABK46159; ABK46159; Mmc1_3674.
DR KEGG; mgm:Mmc1_3674; -.
DR eggNOG; COG0356; Bacteria.
DR HOGENOM; CLU_041018_0_2_5; -.
DR Proteomes; UP000002586; 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; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..259
FT /note="ATP synthase subunit a"
FT /id="PRO_0000362339"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
SQ SEQUENCE 259 AA; 28338 MW; 78B7BD1BD2C32024 CRC64;
MSAEAMHAAA SAAPKMDPLH HFMVQKVVPI EIAGIDLSIT NSTIWMWLAV AVAFLFMKWS
FRGRAEDKLI PTKMQSLAEM TFTFVRQIVD QNIGGAEGRK YFPAIFTLFL LVLFCNLLGL
IPGSFTPTSQ LVVTATLALS VFFFATGLAI VKHGTGFIGF FVPSGVPPML LILMVPIEIV
SYLSRPVSLS VRLFANMTAG HTVLAIMFFF AATLPLGGLL MPAAFATVFT GFELFIGFIQ
AYIFTILTCV YINDALHLH
