ID E0UQU2_SULAO Unreviewed; 505 AA.
AC E0UQU2;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=ATP synthase subunit alpha {ECO:0000256|HAMAP-Rule:MF_01346};
DE EC=7.1.2.2 {ECO:0000256|HAMAP-Rule:MF_01346};
DE AltName: Full=ATP synthase F1 sector subunit alpha {ECO:0000256|HAMAP-Rule:MF_01346};
DE AltName: Full=F-ATPase subunit alpha {ECO:0000256|HAMAP-Rule:MF_01346};
GN Name=atpA {ECO:0000256|HAMAP-Rule:MF_01346};
GN OrderedLocusNames=Saut_0774 {ECO:0000313|EMBL:ADN08823.1};
OS Sulfurimonas autotrophica (strain ATCC BAA-671 / DSM 16294 / JCM 11897 /
OS OK10).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurimonadaceae; Sulfurimonas.
OX NCBI_TaxID=563040 {ECO:0000313|EMBL:ADN08823.1, ECO:0000313|Proteomes:UP000007803};
RN [1] {ECO:0000313|EMBL:ADN08823.1, ECO:0000313|Proteomes:UP000007803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-671 / DSM 16294 / JCM 11897 / OK10
RC {ECO:0000313|Proteomes:UP000007803};
RX PubMed=21304749;
RA Sikorski J., Munk C., Lapidus A., Ngatchou Djao O.D., Lucas S.,
RA Glavina Del Rio T., Nolan M., Tice H., Han C., Cheng J.F., Tapia R.,
RA Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Sims D., Meincke L., Brettin T., Detter J.C.,
RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Rohde M., Lang E., Spring S., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Sulfurimonas autotrophica type strain
RT (OK10).";
RL Stand. Genomic Sci. 3:194-202(2010).
RN [2] {ECO:0000313|Proteomes:UP000007803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-671 / DSM 16294 / JCM 11897 / OK10
RC {ECO:0000313|Proteomes:UP000007803};
RX DOI=10.4056/sigs.1173118;
RA Sikorski J., Munk C., Lapidus A., Djao O., Lucas S., Glavina Del Rio T.,
RA Nolan M., Tice H., Han C., Cheng J., Tapia R., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Sims D.,
RA Meincke L., Brettin T., Detter J., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y., Jeffries C., Rohde M., Lang E., Spring S., Goker M.,
RA Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., Kyrpides N.,
RA Klenk H.;
RT "Complete genome sequence of Sulfurimonas autotrophica type strain
RT (OK10T).";
RL Stand. Genomic Sci. 3:194-202(2010).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The alpha chain is a regulatory subunit.
CC {ECO:0000256|HAMAP-Rule:MF_01346}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01346};
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:0000256|HAMAP-Rule:MF_01346}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_01346}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01346}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|HAMAP-Rule:MF_01346}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002205; ADN08823.1; -; Genomic_DNA.
DR RefSeq; WP_013326579.1; NC_014506.1.
DR AlphaFoldDB; E0UQU2; -.
DR STRING; 563040.Saut_0774; -.
DR KEGG; sua:Saut_0774; -.
DR eggNOG; COG0056; Bacteria.
DR HOGENOM; CLU_010091_2_1_7; -.
DR OrthoDB; 9803053at2; -.
DR Proteomes; UP000007803; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR CDD; cd18113; ATP-synt_F1_alpha_C; 1.
DR CDD; cd18116; ATP-synt_F1_alpha_N; 1.
DR CDD; cd01132; F1-ATPase_alpha_CD; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 1.20.150.20; ATP synthase alpha/beta chain, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR000793; ATP_synth_asu_C.
DR InterPro; IPR038376; ATP_synth_asu_C_sf.
DR InterPro; IPR033732; ATP_synth_F1_a_nt-bd_dom.
DR InterPro; IPR005294; ATP_synth_F1_asu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00962; atpA; 1.
DR PANTHER; PTHR48082; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48082:SF2; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF00306; ATP-synt_ab_C; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 1.
DR SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP-
KW Rule:MF_01346};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01346}; Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01346};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01346};
KW CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|HAMAP-Rule:MF_01346};
KW Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01346};
KW Hydrolase {ECO:0000313|EMBL:ADN08823.1};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW Rule:MF_01346};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01346};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01346}; Reference proteome {ECO:0000313|Proteomes:UP000007803};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW Rule:MF_01346};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01346}.
FT DOMAIN 28..94
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 151..366
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
FT DOMAIN 373..498
FT /note="ATP synthase alpha subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00306"
FT BINDING 171..178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01346"
FT SITE 364
FT /note="Required for activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01346"
SQ SEQUENCE 505 AA; 54765 MW; 9DD2FB0E5EE26343 CRC64;
MVAKIQADEI SSIIKERIDN FELSVDINET GKIVSYADGV AQVYGLSNVM AGEMVEFEDG
TRGLVLNLEE SSVGVVILGA GNALREGMSV KRLGTLLKVP VGDALLGRVV NALGEPIDGK
GPIETTEVRF VEEKAPGIME RKSVHEPLAT GIKAIDALVP IGRGQRELII GDRQTGKTTV
ALDAIINQKG NGVVCIYVAV GQKESTVAQI VRRLEDHGAM EYTIIVSATA AEAAALQFLA
PYTGVTMGEY FRDNARHGLI VYDDLSKHAV AYREMSLILR RPPGREAYPG DVFYVHSRLL
ERAAKLSDEE GAGSLTALPI IETQAGDVAA YIPTNVISIT DGQIFLETDL FNSGVRPAIN
VGLSVSRVGG AAQIKATKQV AGTLRLDLAQ YRELQAFAQF ASDLDEVSRN QLERGQRMVE
VLKQGPFSPL PAEKQVVIIF AGNEGFLDDF DASNVVRFEA ELYPFIEASY PQIFENIRSS
KKVDDETKTL LMKALEEFKA SFVAN
//
