ATPA_PARDP
ID ATPA_PARDP Reviewed; 511 AA.
AC A1B8N8;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=ATP synthase subunit alpha {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 {ECO:0000255|HAMAP-Rule:MF_01346};
DE AltName: Full=F-ATPase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
GN Name=atpA {ECO:0000255|HAMAP-Rule:MF_01346}; OrderedLocusNames=Pden_3816;
OS Paracoccus denitrificans (strain Pd 1222).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=318586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of chromosome 2 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000490; ABL71882.1; -; Genomic_DNA.
DR RefSeq; WP_011750051.1; NC_008687.1.
DR PDB; 5CDF; X-ray; 2.30 A; A=1-511.
DR PDB; 5DN6; X-ray; 3.98 A; A/B/C=1-511.
DR PDBsum; 5CDF; -.
DR PDBsum; 5DN6; -.
DR AlphaFoldDB; A1B8N8; -.
DR SMR; A1B8N8; -.
DR STRING; 318586.Pden_3816; -.
DR TCDB; 3.A.2.1.7; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR PRIDE; A1B8N8; -.
DR EnsemblBacteria; ABL71882; ABL71882; Pden_3816.
DR KEGG; pde:Pden_3816; -.
DR eggNOG; COG0056; Bacteria.
DR HOGENOM; CLU_010091_2_1_5; -.
DR OMA; LQAPGVM; -.
DR Proteomes; UP000000361; Chromosome 2.
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 CDD; cd01132; F1_ATPase_alpha; 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; 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.
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 PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00962; atpA; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; ATP-binding; Cell inner membrane;
KW Cell membrane; CF(1); Hydrogen ion transport; Ion transport; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transport.
FT CHAIN 1..511
FT /note="ATP synthase subunit alpha"
FT /id="PRO_0000302681"
FT BINDING 169..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT SITE 371
FT /note="Required for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT STRAND 26..35
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 151..156
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 175..185
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:5CDF"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 200..208
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 211..224
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 241..260
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 264..270
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 272..285
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 299..308
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 321..329
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 338..344
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 347..353
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 355..359
FT /evidence="ECO:0007829|PDB:5CDF"
FT TURN 368..370
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 372..375
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 376..379
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 382..388
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 391..405
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 413..429
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 439..450
FT /evidence="ECO:0007829|PDB:5CDF"
FT TURN 451..456
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 462..476
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 478..486
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 494..510
FT /evidence="ECO:0007829|PDB:5CDF"
SQ SEQUENCE 511 AA; 55039 MW; FC210B26B95B9322 CRC64;
MGIQAAEISA ILKDQIKNFG QDAEVAEVGQ VLSVGDGIAR VYGLDKVQAG EMVEFPGGIR
GMVLNLETDN VGVVIFGDDR DIKEGDTVKR TGAIVEVPAG KELLGRVVDA LGNPIDGKGP
LNASERRIAD VKAPGIMPRK SVHEPMATGL KSVDAMIPVG RGQRELIIGD RQTGKTAIAL
DTILNQANYN GREADGMKTL HCIYVAVGQK RSTVAQLVKK LEETGAMAYT TVVAATASDP
APMQYLAPYS ATAMGEYFRD NGMDALIIYD DLSKQAVAYR QMSLLLRRPP GREAYPGDVF
YLHSRLLERS AKLNEANGAG SLTALPIIET QAGDVSAYIP TNVISITDGQ IFLETELFFQ
GIRPAVNTGL SVSRVGSAAQ TKAMKSVAGP VKLELAQYRE MAAFAQFGSD LDAATQKLLN
RGARLTELMK QPQYSPLTNA EIVIVIYAGT KGYLDGIPVR DVTKWEHGLL QYLRNQKADL
LEDMTKNDRK VAGELEDAIK AALDGYAKTY A
