ID   ATPA2_POLNA             Reviewed;         520 AA.
AC   A1VPQ8;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=ATP synthase subunit alpha 2 {ECO:0000255|HAMAP-Rule:MF_01346};
DE            EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01346};
DE   AltName: Full=ATP synthase F1 sector subunit alpha 2 {ECO:0000255|HAMAP-Rule:MF_01346};
DE   AltName: Full=F-ATPase subunit alpha 2 {ECO:0000255|HAMAP-Rule:MF_01346};
GN   Name=atpA2 {ECO:0000255|HAMAP-Rule:MF_01346}; OrderedLocusNames=Pnap_2329;
OS   Polaromonas naphthalenivorans (strain CJ2).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=365044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ2;
RX   PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA   Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT   "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT   tar-contaminated sediment, reveals physiological and metabolic versatility
RT   and evolution through extensive horizontal gene transfer.";
RL   Environ. Microbiol. 11:2253-2270(2009).
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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01346}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01346}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01346}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255|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; CP000529; ABM37636.1; -; Genomic_DNA.
DR   RefSeq; WP_011801714.1; NC_008781.1.
DR   AlphaFoldDB; A1VPQ8; -.
DR   SMR; A1VPQ8; -.
DR   STRING; 365044.Pnap_2329; -.
DR   PRIDE; A1VPQ8; -.
DR   EnsemblBacteria; ABM37636; ABM37636; Pnap_2329.
DR   KEGG; pna:Pnap_2329; -.
DR   eggNOG; COG0056; Bacteria.
DR   HOGENOM; CLU_010091_2_1_4; -.
DR   OMA; MLPAIDI; -.
DR   OrthoDB; 837522at2; -.
DR   Proteomes; UP000000644; 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: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   Gene3D; 1.20.150.20; -; 1.
DR   Gene3D; 2.40.30.20; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
DR   InterPro; IPR017710; Alt_ATP_synth_F1_asu.
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; 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   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF00306; ATP-synt_ab_C; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   SUPFAM; SSF50615; SSF50615; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR03324; alt_F1F0_F1_al; 1.
DR   TIGRFAMs; TIGR00962; atpA; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; ATP-binding; Cell inner membrane; Cell membrane; CF(1);
KW   Hydrogen ion transport; Ion transport; Membrane; Nucleotide-binding;
KW   Reference proteome; Translocase; Transport.
FT   CHAIN           1..520
FT                   /note="ATP synthase subunit alpha 2"
FT                   /id="PRO_0000339045"
FT   BINDING         176..183
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT   SITE            369
FT                   /note="Required for activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
SQ   SEQUENCE   520 AA;  55829 MW;  1095C456A55C84EA CRC64;
     MSAPADTLKS ALDRTFASLR HGLETYTAQL TPHEVGTITR VSTGIAMVSG LPGVGFEELV
     SFSGNVFGIA FNVDETEIGV VLLGDYGHLH AGDPVRRTGR VMDVAVGEGL LGRVIDPLGR
     PLDSLGPVVS SARLALERPA APIMDRAPVT VPLQTGLKVV DALIPIGRGQ RELILGDRQT
     GKTAIAVDTI LNQRGQDVLC VYCAIGQRAA AVARTIAVLR EKGAMEYTVV VVTEGNDPPG
     LAYIAPYAAT SIAEHFMEMG RDVLVVYDDL TQHARAYREL SLLLRRPPGR EAFPGDIFYI
     HSRLLERATH LRPERGGGSL TALPIIETEA QNMSAYIPTN LISITDGQIY LSPSLFELGV
     LPAVDVSKSV SRVGGKAQRA AYRAVTGDLK LAYAQFEELE TFARFGARLD ENTQKIIEHG
     RRIRACLQQP ESAPVSMAGQ ITVLLALTAA FFDGVPLARM TAAEQAVLQA AATLPAELQT
     RFDTAMKLSE ADRATLIQLA RDALKPFVPP PAESRRTSAP