ATPB_STRP4
ID ATPB_STRP4 Reviewed; 468 AA.
AC B5E670;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=SPG_1430;
OS Streptococcus pneumoniae serotype 19F (strain G54).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=512566;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G54;
RX PubMed=11442348; DOI=10.1089/10766290152044995;
RA Dopazo J., Mendoza A., Herrero J., Caldara F., Humbert Y., Friedli L.,
RA Guerrier M., Grand-Schenk E., Gandin C., de Francesco M., Polissi A.,
RA Buell G., Feger G., Garcia E., Peitsch M., Garcia-Bustos J.F.;
RT "Annotated draft genomic sequence from a Streptococcus pneumoniae type 19F
RT clinical isolate.";
RL Microb. Drug Resist. 7:99-125(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G54;
RA Mulas L., Trappetti C., Hakenbeck R., Iannelli F., Pozzi G., Davidsen T.M.,
RA Tettelin H., Oggioni M.;
RT "Pneumococcal beta glucoside metabolism investigated by whole genome
RT comparison.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001015; ACF55583.1; -; Genomic_DNA.
DR RefSeq; WP_000094363.1; NC_011072.1.
DR KEGG; spx:SPG_1430; -.
DR HOGENOM; CLU_022398_0_2_9; -.
DR OMA; GFNMIMD; -.
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; Translocase; Transport.
FT CHAIN 1..468
FT /note="ATP synthase subunit beta"
FT /id="PRO_1000143552"
FT BINDING 155..162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ SEQUENCE 468 AA; 50898 MW; B7FA699CD2CD6FBD CRC64;
MSSGKIAQVI GPVVDVLFAA GEKLPEINNA LVVYKNDERK TKIVLEVALE LGDGMVRTIA
MESTDGLTRG MEVLDTGRPI SVPVGKETLG RVFNVLGDTI DLEAPFTEDA ERQPIHKKAP
TFDELSTSSE ILETGIKVID LLAPYLKGGK VGLFGGAGVG KTVLIQELIH NIAQEHGGIS
VFTGVGERTR EGNDLYWEMK ESGVIEKTAM VFGQMNEPPG ARMRVALTGL TIAEYFRDVE
GQDVLLFIDN IFRFTQAGSE VSALLGRMPS AVGYQPTLAT EMGQLQERIT STKKGSVTSI
QAIYVPADDY TDPAPATAFA HLDSTTNLER KLVQLGIYPA VDPLASSSRA LAPEIVGEEH
YAVAAEVKRV LQRYHELQDI IAILGMDELS DEEKTLVARA RRIQFFLSQN XNVAEQFTGQ
PGSYVPVAET VRGFKEILDG KYDHLPEDAF RGVGSIEDVI AKAEKMGF