ATPA2_ACAM1
ID ATPA2_ACAM1 Reviewed; 513 AA.
AC A8ZNS4;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=AM1_D0165;
OS Acaryochloris marina (strain MBIC 11017).
OG Plasmid pREB4.
OC Bacteria; Cyanobacteria; Synechococcales; Acaryochloridaceae;
OC Acaryochloris.
OX NCBI_TaxID=329726;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBIC 11017;
RX PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA Blankenship R.E., Touchman J.W.;
RT "Niche adaptation and genome expansion in the chlorophyll d-producing
RT cyanobacterium Acaryochloris marina.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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 four main
CC subunits: a(1), b(1), b'(1) and c(9-12) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid 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}.
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DR EMBL; CP000841; ABW32660.1; -; Genomic_DNA.
DR RefSeq; WP_012167716.1; NC_009929.1.
DR AlphaFoldDB; A8ZNS4; -.
DR SMR; A8ZNS4; -.
DR EnsemblBacteria; ABW32660; ABW32660; AM1_D0165.
DR KEGG; amr:AM1_D0165; -.
DR HOGENOM; CLU_010091_2_1_3; -.
DR OMA; VICIYCA; -.
DR OrthoDB; 837522at2; -.
DR Proteomes; UP000000268; Plasmid pREB4.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid 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; CF(1); Hydrogen ion transport; Ion transport;
KW Membrane; Nucleotide-binding; Plasmid; Reference proteome; Thylakoid;
KW Translocase; Transport.
FT CHAIN 1..513
FT /note="ATP synthase subunit alpha 2"
FT /id="PRO_0000339010"
FT BINDING 177..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT SITE 370
FT /note="Required for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
SQ SEQUENCE 513 AA; 56506 MW; 42377C6FD1D13827 CRC64;
MEAPKLDILK PVLQHIFAAF DQVEGEYPFE LQSQEIGIVT SLGHGIARAT GLLQVQSEEL
VKFPGDRMGL AFNLDPDEVG LILLDDGHSL KAGCEVQRTG RVLDVPVGEG LLGRVVDATG
RPLDQRGLVT AQERRPVERE APAIMDRAPV TVPLQTGIKA IDALIPIGRG QRELIVGDRQ
TGKTAIAVDT ILNQKDQDVI CVYCAIGQRS SAVAKLIAEL RNRGAMDYCI VVVAEGEASP
GLQYITPYAA TTMAEYFMEQ GQDVLIVYDD LIQHARAYRE LSLLLRRPPG REAFPGDIFY
IHARLLERAT CLRPELGGGS LTALPIVETE AQNLSAYIPT NLVSITDGQI YLTPDLFQKG
IFPAVDVGKS VSRVGGKAQL PAYRDVAGDL RLSYTQFEEL ESFARFGTRL EESTRQSLER
GRRVREVLQQ PQFQPLPVAE QIAVMLAVTQ GQFDLVPIEQ VSQAQQLIGE AIRRELPNIC
DRIQNAGQLS ETDRETLLNW IANHILKDSD NEL
