ATP6_SYNSC
ID ATP6_SYNSC Reviewed; 241 AA.
AC Q3AHK0;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 100.
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 Synonyms=atpI {ECO:0000255|HAMAP-Rule:MF_01393};
GN OrderedLocusNames=Syncc9605_2193;
OS Synechococcus sp. (strain CC9605).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=110662;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9605;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9605.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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 four main
CC subunits: a, b, b' and c. {ECO:0000255|HAMAP-Rule:MF_01393}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid 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; CP000110; ABB35932.1; -; Genomic_DNA.
DR RefSeq; WP_006852023.1; NC_007516.1.
DR AlphaFoldDB; Q3AHK0; -.
DR SMR; Q3AHK0; -.
DR STRING; 110662.Syncc9605_2193; -.
DR EnsemblBacteria; ABB35932; ABB35932; Syncc9605_2193.
DR KEGG; syd:Syncc9605_2193; -.
DR eggNOG; COG0356; Bacteria.
DR HOGENOM; CLU_041018_2_4_3; -.
DR OMA; FTHAVRL; -.
DR OrthoDB; 867266at2; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid 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; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..241
FT /note="ATP synthase subunit a"
FT /id="PRO_0000362486"
FT TRANSMEM 30..50
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 128..148
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
SQ SEQUENCE 241 AA; 27097 MW; 87B1B40550D23BD9 CRC64;
MALLPLPLPF AELEVGHHLY WQIGDLYLHG QVFLSSWILI GILLAVVLVG TRGMKRDPIG
LQNLLEFLWN FIRDIARDNI GEKYYRDWLP FIGTLFLFIF VSNWGGALIP WKIFELPEGE
LGAPTADINT TVAMALLVSL AYFYAGLSRK GLRFFELYVE PTPIMLPFKI IEEFTKPLSL
SFRLFGNILA DELAVGVLVY LVPLIVPLPV MLLGLFTSAI QALIFATLAS FYIGEGLHEA
H