ID   A0A143LSQ6_LEPBO        Unreviewed;       503 AA.
AC   A0A143LSQ6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   07-SEP-2016, entry version 3.
DE   RecName: Full=ATP synthase subunit alpha {ECO:0000256|HAMAP-Rule:MF_01346};
DE            EC=3.6.3.14 {ECO:0000256|HAMAP-Rule:MF_01346};
DE   AltName: Full=ATP synthase F1 sector subunit alpha {ECO:0000256|HAMAP-Rule:MF_01346};
DE   AltName: Full=F-ATPase subunit alpha {ECO:0000256|HAMAP-Rule:MF_01346};
GN   Name=atpA {ECO:0000256|HAMAP-Rule:MF_01346};
GN   ORFNames=LBHA_10265 {ECO:0000313|EMBL:AMX68433.1}, LBHB_09425
GN   {ECO:0000313|EMBL:AMX71484.1};
OS   Leptospira borgpetersenii serovar Hardjo.
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=328971 {ECO:0000313|EMBL:AMX71484.1};
RN   [1] {ECO:0000313|EMBL:AMX71484.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NVSL S 1343 {ECO:0000313|EMBL:AMX68433.1}, and NVSL S 818
RC   {ECO:0000313|EMBL:AMX71484.1};
RA   Llanes A., Restrepo C., Rajeev S.;
RT   "Genomic differences between Leptospira borgpetersenii serovar Hardjo
RT   laboratory strains and field isolates.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|HAMAP-Rule:MF_01346}.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate +
CC       H(+)(Out). {ECO:0000256|HAMAP-Rule:MF_01346}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01346}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01346}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|HAMAP-Rule:MF_01346}.
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DR   EMBL; CP015050; AMX68433.1; -; Genomic_DNA.
DR   EMBL; CP015052; AMX71484.1; -; Genomic_DNA.
DR   RefSeq; WP_011670484.1; NZ_CP015052.1.
DR   GeneID; 4408290; -.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0046933; F:proton-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   CDD; cd01132; F1_ATPase_alpha; 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; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR023366; ATPase_asu-like.
DR   InterPro; IPR005294; ATPase_F1-cplx_asu.
DR   InterPro; IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR004100; ATPase_F1_a/bsu_N.
DR   InterPro; IPR033732; F1_ATPase_alpha.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR15184:SF3; PTHR15184:SF3; 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   PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 1.
DR   SUPFAM; SSF47917; SSF47917; 1.
DR   SUPFAM; SSF50615; SSF50615; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00962; atpA; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis {ECO:0000256|HAMAP-Rule:MF_01346};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01346};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01346};
KW   CF(1) {ECO:0000256|HAMAP-Rule:MF_01346};
KW   Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01346};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01346};
KW   Ion transport {ECO:0000256|HAMAP-Rule:MF_01346};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01346};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01346};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01346}.
FT   DOMAIN       26     91       ATP-synt_ab_N. {ECO:0000259|Pfam:
FT                                PF02874}.
FT   DOMAIN      149    365       ATP-synt_ab. {ECO:0000259|Pfam:PF00006}.
FT   DOMAIN      372    487       ATP-synt_ab_C. {ECO:0000259|Pfam:
FT                                PF00306}.
FT   NP_BIND     169    176       ATP. {ECO:0000256|HAMAP-Rule:MF_01346}.
FT   SITE        363    363       Required for activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_01346}.
SQ   SEQUENCE   503 AA;  54937 MW;  C7413A98F8828EEC CRC64;
     MKIKTDEITS VLKQEILNYK KDLGVDEVGT VLEIGDGIAR VYGLKNVMSG EMVEFQNGIF
     GQAFNLEDNS VGVVVYGDYL AIQEGFTVKR TSRILEVPVG PELLGRVVNP LGEPLDGKGP
     INAKLTRPVE SPAPGIAMRQ PVGEPMQTGI KAIDAMIPIG RGQRELIIGD RGTGKTSIAL
     DTIINQKGTG VICVYVAIGQ KASTVASTVE MLRNKGALEY TIVVSATAAE PAPLQYIAPY
     SGCSMAEYFM YNEKKATLVV YDDLSKQAVA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE
     RAAKLDDKYG AGSLTALPII ETQEGEVSAY IPTNVISITD GQIYLQSNLF ASGNRPAVDV
     GISVSRVGSA AQIKAMKQVA GKMKLELAQF RDLEAFAQLG TELDPATQAQ LDRGNRIVQM
     LKQPVSSPFP VEEQVVEIFA VTRGFMDKIP VPKVQQYGKF LLTRIKEQHS EVLEAIRKEK
     KISDEEKLGE VLSAIAEEFL RKH
//