ATP6_SULDN
ID ATP6_SULDN Reviewed; 224 AA.
AC Q30QW4;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-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}; OrderedLocusNames=Suden_1339;
OS Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira
OS denitrificans (strain ATCC 33889 / DSM 1251)).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Thiovulaceae; Sulfurimonas.
OX NCBI_TaxID=326298;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33889 / DSM 1251;
RX PubMed=18065616; DOI=10.1128/aem.01844-07;
RA Sievert S.M., Scott K.M., Klotz M.G., Chain P.S.G., Hauser L.J., Hemp J.,
RA Huegler M., Land M., Lapidus A., Larimer F.W., Lucas S., Malfatti S.A.,
RA Meyer F., Paulsen I.T., Ren Q., Simon J., Bailey K., Diaz E.,
RA Fitzpatrick K.A., Glover B., Gwatney N., Korajkic A., Long A.,
RA Mobberley J.M., Pantry S.N., Pazder G., Peterson S., Quintanilla J.D.,
RA Sprinkle R., Stephens J., Thomas P., Vaughn R., Weber M.J., Wooten L.L.;
RT "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas
RT denitrificans.";
RL Appl. Environ. Microbiol. 74:1145-1156(2008).
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; CP000153; ABB44617.1; -; Genomic_DNA.
DR RefSeq; WP_011372969.1; NC_007575.1.
DR AlphaFoldDB; Q30QW4; -.
DR SMR; Q30QW4; -.
DR STRING; 326298.Suden_1339; -.
DR EnsemblBacteria; ABB44617; ABB44617; Suden_1339.
DR KEGG; tdn:Suden_1339; -.
DR eggNOG; COG0356; Bacteria.
DR HOGENOM; CLU_041018_2_2_7; -.
DR OMA; ITIVYYH; -.
DR OrthoDB; 867266at2; -.
DR Proteomes; UP000002714; 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; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..224
FT /note="ATP synthase subunit a"
FT /id="PRO_0000362479"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
SQ SEQUENCE 224 AA; 25369 MW; 30AE4517F862FDE1 CRC64;
MGELFTFFGL ISHDKTFIYM THMLLAAGIA LMLVKMAMSN LKVVPTGTQN VMEAYISGVL
KMGTDVMGQE AARRYLPLVA TIGLFVGIAN LIGVVPGFEA PTAFLEFAFT LALSVFIYYN
YEGIRRQGVV KYFKHFLGPV WWLYWLMFPI EIVSHFSRLV SLSFRLFGNV KGDDMFLMVI
LMLAPWVLPM IPYALLTFMA FLQAFIFMML TYVYLGSAIA VEEH
