ATPB_LACAC
ID ATPB_LACAC Reviewed; 479 AA.
AC Q5FKY0; Q9RGY1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=ATP synthase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
DE EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01347};
DE AltName: Full=ATP synthase F1 sector subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
DE AltName: Full=F-ATPase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
GN Name=atpD {ECO:0000255|HAMAP-Rule:MF_01347}; OrderedLocusNames=LBA0778;
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 catalytic sites are hosted primarily by the
CC beta subunits. {ECO:0000255|HAMAP-Rule:MF_01347}.
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_01347};
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_01347}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01347};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01347}.
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_01347}.
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DR EMBL; AF098522; AAF22498.1; -; Genomic_DNA.
DR EMBL; CP000033; AAV42644.1; -; Genomic_DNA.
DR RefSeq; WP_011254247.1; NC_006814.3.
DR RefSeq; YP_193675.1; NC_006814.3.
DR AlphaFoldDB; Q5FKY0; -.
DR SMR; Q5FKY0; -.
DR STRING; 272621.LBA0778; -.
DR PRIDE; Q5FKY0; -.
DR EnsemblBacteria; AAV42644; AAV42644; LBA0778.
DR KEGG; lac:LBA0778; -.
DR PATRIC; fig|272621.13.peg.740; -.
DR eggNOG; COG0055; Bacteria.
DR HOGENOM; CLU_022398_0_2_9; -.
DR OMA; GFNMIMD; -.
DR BioCyc; LACI272621:G1G49-794-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 Gene3D; 1.10.1140.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01347; ATP_synth_beta_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005722; ATP_synth_F1_bsu.
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; IPR024034; ATPase_F1/V1_b/a_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01039; atpD; 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..479
FT /note="ATP synthase subunit beta"
FT /id="PRO_0000254278"
FT BINDING 153..160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
FT CONFLICT 104
FT /note="F -> L (in Ref. 1; AAF22498)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="D -> N (in Ref. 1; AAF22498)"
FT /evidence="ECO:0000305"
FT CONFLICT 128..129
FT /note="EI -> KN (in Ref. 1; AAF22498)"
FT /evidence="ECO:0000305"
FT CONFLICT 165..166
FT /note="EL -> KI (in Ref. 1; AAF22498)"
FT /evidence="ECO:0000305"
FT CONFLICT 276..279
FT /note="LATE -> ITR (in Ref. 1; AAF22498)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="V -> E (in Ref. 1; AAF22498)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 479 AA; 52215 MW; 51B4A94A99CB58C0 CRC64;
MSEGEIVQVI GPVVDVKFPI DKNLPDINNA LRVIKSEDES IVLEVTLELG DGVLRTIAME
STDGLRRGMK VEDTGAPISV PVGEDTLGRV FNVLGQPIDG GPAFPKDHPR EGIHKEAPKY
EDLTTSREIL ETGIKVIDLL EPYVRGGKVG LFGGAGVGKT TIIQELIHNI AQEHGGISVF
TGVGERTREG NDLYFEMKAS GVLSKTAMVF GQMNEPPGAR MRVALTGLTL AEYFRDVEGQ
DVLLFIDNIF RFTQAGSEVS ALLGRMPSAV GYQPTLATEM GQLQERITST KKGSITSIQA
VYVPADDYTD PAPSTTFAYL DATTNLERSL VEQGIYPAVD PLESSSSALD PEVVGQEHYE
VATRVQHVLQ RYHELQDIIS VLGMDELSDE EKLIVARARK VQFFLSQNFF VAEQFTGVPG
SYVPIKETIK GFKLILDGHL DDLPEDAFRG VGPIEDVLKK AQEMGVTPSD PEAKALLEK
