(data stored in ACNUC7421 zone)

HOGENOM: FRASN_1_PE1009

ID   FRASN_1_PE1009                       STANDARD;      PRT;   553 AA.
AC   FRASN_1_PE1009; A8L3W3;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=ATP synthase subunit alpha; EC=3.6.3 14;AltName: Full=ATP
DE   synthase F1 sector subunit alpha;AltName: Full=F-ATPase subunit alpha;
DE   (FRASN_1.PE1009).
GN   Name=atpA; OrderedLocusNames=Franean1_1022;
OS   FRANKIA SP. EAN1PEC.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Frankineae;
OC   Frankiaceae; Frankia.
OX   NCBI_TaxID=298653;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS FRASN_1.PE1009.
CC       Frankia sp. EAN1pec, complete genome.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:ATPA_FRASN
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton
CC       gradient across the membrane. The alpha chain is a regulatory
CC       subunit (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate +
CC       H(+)(Out).
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC       core - and CF(0) - the membrane proton channel. CF(1) has five
CC       subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
CC       has three main subunits: a(1), b(2) and c(9-12). The alpha and
CC       beta chains form an alternating ring which encloses part of the
CC       gamma chain. CF(1) is attached to CF(0) by a central stalk formed
CC       by the gamma and epsilon chains, while a peripheral stalk is
CC       formed by the delta and b chains (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC   -!- GENE_FAMILY: HOG000130111 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A8L3W3; -.
DR   EMBL; CP000820; ABW10478.1; -; Genomic_DNA.
DR   RefSeq; YP_001505384.1; NC_009921.1.
DR   ProteinModelPortal; A8L3W3; -.
DR   SMR; A8L3W3; 31-513.
DR   STRING; A8L3W3; -.
DR   GeneID; 5669436; -.
DR   GenomeReviews; CP000820_GR; Franean1_1022.
DR   KEGG; fre:Franean1_1022; -.
DR   OMA; GSDRDIK; -.
DR   ProtClustDB; PRK09281; -.
DR   BioCyc; FSP1855:FRANEAN1_1022-MON; -.
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-KW.
DR   GO; GO:0046933; F:hydrogen ion transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
DR   HAMAP; MF_01346; ATP_synth_alpha_bact; 1; -.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR005294; ATPase_F1-cplx_asu.
DR   InterPro; IPR018118; ATPase_F1/A1-cplx_a/bsu_N.
DR   InterPro; IPR023366; ATPase_F1/A1-cplx_a_su_N.
DR   InterPro; IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C.
DR   InterPro; IPR004100; ATPase_F1/V1/A1-cplx_a/bsu_N.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   Gene3D; G3DSA:2.40.30.20; G3DSA:2.40.30.20; 1.
DR   PANTHER; PTHR15184:SF3; ATPase_F1_a; 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   SUPFAM; SSF47917; ATPase_a/b_C; 1.
DR   SUPFAM; SSF50615; ATPase_a/b_N; 1.
DR   TIGRFAMs; TIGR00962; AtpA; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
DR   HOGENOMDNA; FRASN_1.PE1009; -.
KW   F0F1 ATP synthase subunit alpha;
KW   ATP synthesis; ATP-binding; Cell membrane; CF(1); Complete proteome;
KW   Hydrogen ion transport; Hydrolase; Ion transport; Membrane;
KW   Nucleotide-binding; Transport.
SQ   SEQUENCE   553 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTELSIRPEE IRDALREYVD SFQATSGDRE EVGRVVVTGD GIARVEGLPH TMTNELLEFS
     GGVLGLALNL EVGEIGCVIL GDAEHIEEGQ EVRRTGEILA VPVGDGFLGR VVDPLGRPID
     GLGDIAAAGT RALELQAPSV VQRQPVKEPL QTGIKAIDAM TAIGRGQRQL IIGDRQTGKT
     TVAIDAIINQ RDNWASGDPK KQVKCVYVAI GQKKTTIREV VNTLEEAGAL AYTTIVAAPA
     DQPAGFKYIA PYTGSAIGQY WMYNGQHSLV VFDDLSKQAE AYRAISLLLR RPPGREAYPG
     DVFYLHSRLL ERCAKLSDEL GGGSLTGLPI IETKANDISA YIPTNVISIT DGQIFLESDL
     FNQGVRPAIN VGTSVSRVGG SAQVKAMKSV AGRLRLDLAQ YRELEAFSAF GSDLDKASRD
     QLARGARLVE LLKQPQNKPF SVERQVVSIW AGTTGKLDDV PVEDIRRFEA EFLDFVGRTH
     GAIYDTIVNT GKLGDDLVSS LESAIAEFKE QFTLSSGKQL VNEAAPEALD PSAVEREEIA
     VHHRKPSDET AGH
//

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