ATPA_LACLA
ID ATPA_LACLA Reviewed; 500 AA.
AC Q9CER8; Q93MY8; Q9RAU2;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
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=LL1766;
GN ORFNames=L8990;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CHCC373;
RA Pedersen M.B., Kragelund L., Jensen P.R., Nilsson D.;
RT "Sequence of the atp operon from Lactococcus lactis subsp. lactis
RT CHCC373.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C2;
RA Ishikawa K., Fujii R., Tomita F., Yokota A.;
RT "Lactococcus lactis subsp. lactis C2 H+-ATPase operon.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(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; AF393838; AAK84017.1; -; Genomic_DNA.
DR EMBL; AB072443; BAB69469.1; -; Genomic_DNA.
DR EMBL; AE005176; AAK05864.1; -; Genomic_DNA.
DR PIR; F86845; F86845.
DR RefSeq; NP_267922.1; NC_002662.1.
DR RefSeq; WP_004255265.1; NC_002662.1.
DR AlphaFoldDB; Q9CER8; -.
DR SMR; Q9CER8; -.
DR STRING; 272623.L8990; -.
DR PaxDb; Q9CER8; -.
DR EnsemblBacteria; AAK05864; AAK05864; L8990.
DR GeneID; 60355761; -.
DR GeneID; 66442752; -.
DR KEGG; lla:L8990; -.
DR PATRIC; fig|272623.7.peg.1893; -.
DR eggNOG; COG0056; Bacteria.
DR HOGENOM; CLU_010091_2_1_9; -.
DR OMA; LQAPGVM; -.
DR Proteomes; UP000002196; 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 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; 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.
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..500
FT /note="ATP synthase subunit alpha"
FT /id="PRO_0000144332"
FT BINDING 169..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT SITE 362
FT /note="Required for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT CONFLICT 59
FT /note="V -> I (in Ref. 2; BAB69469)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="C -> W (in Ref. 1; AAK84017)"
FT /evidence="ECO:0000305"
FT CONFLICT 447
FT /note="D -> N (in Ref. 2; BAB69469)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="E -> D (in Ref. 2; BAB69469)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="E -> D (in Ref. 2; BAB69469)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 500 AA; 54325 MW; 49139BB00264F49B CRC64;
MAIKANEISS LIKKQIENFT PDFEVAETGV VTYVGDGIAR AYGLENAMSG ELVEFSNGVL
GMAQNLDATD VGIIVLGDFL SIREGDTVKR TGKIMEIQVG EELIGRVVNP LGQPVDGLGE
LNTGKTRPVE AKAPGVMQRK SVSEPLQTGL KAIDALVPIG RGQRELIIGD RQTGKTSVAI
DAILNQKGQD MICIYVAIGQ KESTVRTQVE TLRKLGAMDY TIVVTASASQ PSPLLYIAPY
AGAAMGEEFM YNGKHVLVVY DDLSKQAVAY RELSLLLRRP PGREAYPGDV FYLHSRLLER
AAKLSDDLGG GSMTALPFIE TQAGDISAYI ATNVISITDG QIFLENDLFY SGVRPAIDAG
SSVSRVGGAA QIKAMKKVAG TLRLDLASFR ELEAFTQFGS DLDEATQAKL NRGRRTVEVL
KQPLHKPLAV EKQVLILYAL THGHLDDVPV DDVLDFETKM FDFFDANYAE LLNVITETKD
LPEEAKLDEA IKAFKNTTNY
