ID   ATPA2_MYCPU             Reviewed;         513 AA.
AC   Q98QB7;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 1.
DT   03-AUG-2022, entry version 131.
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=MYPU_4490;
OS   Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=272635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAB CTIP;
RX   PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA   Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA   Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT   "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT   pulmonis.";
RL   Nucleic Acids Res. 29:2145-2153(2001).
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 membrane {ECO:0000255|HAMAP-Rule:MF_01346};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01346}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255|HAMAP-Rule:MF_01346}.
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DR   EMBL; AL445564; CAC13622.1; -; Genomic_DNA.
DR   PIR; A99568; A99568.
DR   RefSeq; WP_010925250.1; NC_002771.1.
DR   AlphaFoldDB; Q98QB7; -.
DR   SMR; Q98QB7; -.
DR   STRING; 272635.MYPU_4490; -.
DR   EnsemblBacteria; CAC13622; CAC13622; CAC13622.
DR   KEGG; mpu:MYPU_4490; -.
DR   eggNOG; COG0056; Bacteria.
DR   HOGENOM; CLU_010091_0_0_14; -.
DR   OMA; ANNMDAD; -.
DR   OrthoDB; 1619125at2; -.
DR   BioCyc; MPUL272635:G1GT6-454-MON; -.
DR   Proteomes; UP000000528; 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   HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
DR   InterPro; IPR000793; ATP_synth_asu_C.
DR   InterPro; IPR005294; ATP_synth_F1_asu.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
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   SUPFAM; SSF50615; SSF50615; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; ATP-binding; Cell membrane; CF(1); Hydrogen ion transport;
KW   Ion transport; Membrane; Nucleotide-binding; Reference proteome;
KW   Translocase; Transport.
FT   CHAIN           1..513
FT                   /note="ATP synthase subunit alpha 2"
FT                   /id="PRO_0000144338"
FT   BINDING         152..159
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT   SITE            341
FT                   /note="Required for activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
SQ   SEQUENCE   513 AA;  58129 MW;  D0E19C8CDEB9A4E9 CRC64;
     MDNAKIVIKS IKDYIVEVQG DYDFRLYEVF QLTDDVKGFC LSVDEKRTFL LIDGDTSKIK
     VGTEIIPLES RFIAKTYKDY FGKIIDIDGK VLYSESEDQE ISEKAYENEN SAFKVASGIQ
     DRVKLNEPLE TGIFSIDILL PIGKGQRQLI LGDSKTGKTS IALSTMINQK ENDIKIIYVS
     IGLKSNDLKR IYKTIVEQKI AHKTILMHAS SDNSFQQFLI PYVAMAHAEN IMQSGEDVLI
     IFDDLTNHAN VLREIALLTG KPVGKEAFPG DLFYSHSKLL ERAGKFKNGY SITCFPIVRT
     INNDMTSLLA SNIASITDGQ IVTNSEIKDQ GILPAIDIGL SVSRTGSSVQ SVSLSKIAIE
     ISKIYSKYKQ NEKFSDTNFD LNDSVRDIIK KGKILLKILN QKEFQAYSRS FNLIIAYIVV
     WGIFEDEEKI YDKLIYLYFV LRYDYIGKIL VNVVDKKSGV DGMVDEGVLK AEIMRLLAHF
     KDIHNIKTKS YNDGKFNLST RVLHKVKDRI WEK