ATPB_LACLA
ID ATPB_LACLA Reviewed; 469 AA.
AC Q9CES0; Q93MY7; Q9RAU0;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
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=LL1764;
GN ORFNames=L6563;
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 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 -!- 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 -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01347}.
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DR EMBL; AF393838; AAK84019.1; -; Genomic_DNA.
DR EMBL; AB072443; BAB69471.1; -; Genomic_DNA.
DR EMBL; AE005176; AAK05862.1; -; Genomic_DNA.
DR PIR; D86845; D86845.
DR RefSeq; NP_267920.1; NC_002662.1.
DR RefSeq; WP_010906126.1; NC_002662.1.
DR AlphaFoldDB; Q9CES0; -.
DR SMR; Q9CES0; -.
DR STRING; 272623.L6563; -.
DR PaxDb; Q9CES0; -.
DR EnsemblBacteria; AAK05862; AAK05862; L6563.
DR GeneID; 60355780; -.
DR KEGG; lla:L6563; -.
DR PATRIC; fig|272623.7.peg.1890; -.
DR eggNOG; COG0055; Bacteria.
DR HOGENOM; CLU_022398_0_2_9; -.
DR OMA; GFNMIMD; -.
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 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 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..469
FT /note="ATP synthase subunit beta"
FT /id="PRO_0000144448"
FT BINDING 156..163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
FT CONFLICT 9
FT /note="I -> V (in Ref. 2; BAB69471)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="A -> S (in Ref. 2; BAB69471)"
FT /evidence="ECO:0000305"
FT CONFLICT 106..108
FT /note="EFA -> DFP (in Ref. 2; BAB69471)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="E -> A (in Ref. 2; BAB69471)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 50911 MW; 43BCD676E7A1EB0F CRC64;
MSSGKITQII GPVVDVEFGS DAKLPEINNA LIVYKDVNGL KTKITLEVAL ELGDGAVRTI
AMESTDGLTR GLEVLDTGKA VSVPVGEATL GRVFNVLGDV IDGGEEFAAD AERNPIHKKA
PTFDELSTAN EVLVTGIKVV DLLAPYLKGG KVGLFGGAGV GKTVLIQELI HNIAQEHGGI
SVFTGVGERT REGNDLYWEM KESGVIEKTA MVFGQMNEPP GARMRVALTG LTIAEYFRDV
QGQDVLLFID NIFRFTQAGS EVSALLGRMP SAVGYQPTLA TEMGQLQERI TSTKKGSVTS
IQAIYVPADD YTDPAPATAF AHLDATTNLE RRLTQMGIYP AVDPLASSSR ALTPEIVGEE
HYEVAMEVQR VLQRYKELQD IIAILGMDEL SDDEKILVGR ARRIQFFLSQ NFHVAEQFTG
QPGSYVPIDK TVHDFKEILE GKYDEVPEDA FRGVGPIEDV LEKAKSMGY
