ATPA_LACAC
ID ATPA_LACAC Reviewed; 503 AA.
AC Q5FKY2; Q9RGY3;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=LBA0776;
OS Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=272621;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ACTIVITY REGULATION, INDUCTION, AND
RP PROBABLE OPERON.
RC STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX PubMed=10510230; DOI=10.1046/j.1365-2958.1999.01557.x;
RA Kullen M.J., Klaenhammer T.R.;
RT "Identification of the pH-inducible, proton-translocating F1F0-ATPase
RT (atpBEFHAGDC) operon of Lactobacillus acidophilus by differential display:
RT gene structure, cloning and characterization.";
RL Mol. Microbiol. 33:1152-1161(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA Hamrick A., Cano R., Klaenhammer T.R.;
RT "Complete genome sequence of the probiotic lactic acid bacterium
RT Lactobacillus acidophilus NCFM.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
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 -!- ACTIVITY REGULATION: Increases 2-fold following exposure to low pH.
CC {ECO:0000269|PubMed:10510230}.
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 -!- INDUCTION: By low pH. {ECO:0000269|PubMed:10510230}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01346}.
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DR EMBL; AF098522; AAF22496.1; -; Genomic_DNA.
DR EMBL; CP000033; AAV42642.1; -; Genomic_DNA.
DR RefSeq; WP_011254246.1; NC_006814.3.
DR RefSeq; YP_193673.1; NC_006814.3.
DR AlphaFoldDB; Q5FKY2; -.
DR SMR; Q5FKY2; -.
DR STRING; 272621.LBA0776; -.
DR PRIDE; Q5FKY2; -.
DR EnsemblBacteria; AAV42642; AAV42642; LBA0776.
DR GeneID; 56942403; -.
DR KEGG; lac:LBA0776; -.
DR PATRIC; fig|272621.13.peg.738; -.
DR eggNOG; COG0056; Bacteria.
DR HOGENOM; CLU_010091_2_1_9; -.
DR OMA; LQAPGVM; -.
DR BioCyc; LACI272621:G1G49-792-MON; -.
DR Proteomes; UP000006381; 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; 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 2: Evidence at transcript level;
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..503
FT /note="ATP synthase subunit alpha"
FT /id="PRO_0000238265"
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 402
FT /note="L -> P (in Ref. 1; AAF22496)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 503 AA; 54932 MW; 4712C0D1F6AA8916 CRC64;
MSIKAEEISS LIKQQLEHYD DKLDINEVGV VTYVGDGIAR AHGLDDVLSG ELLKFDNGSF
GIAQNLESND VGIIILGQFD NIREGDRVQR TGRIMEVPVG DALIGRVVNP LGQPVDGLGE
IKSDKTRPIE AKAPGVMDRQ SVNQPLQTGI KAIDALVPIG RGQRELIIGD RKTGKTSLAI
DTILNQKGQD VICIYVAIGQ KESTVRTQVE TLKRFGAMDY TIVVEAGPSE PAPMLYIAPY
AGTAMGEEFM YNGKDVLIVF DDLSKQAVAY RELSLLLRRP PGREAYPGDV FYLHSRLLER
SAKLSDKLGG GSLTALPIIQ TEAGDISAYI PTNVISITDG QIFLQSDLFF AGTRPAIDAG
NSVSRVGGNA QIKAMKKVAG TLRTDLTAYR ELESFAQFGS DLDQATQAKL NRGQRTVEVL
KQPLHDPIPV EKQVLILYAL THGYLDAIPV EDISRFQNEL FDNFDSSHAD LLKTIRETGK
LPDDKELSAA IEEFSESFTP SEK
