ATPB_NOSS1
ID ATPB_NOSS1 Reviewed; 482 AA.
AC P06540;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 152.
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};
GN Synonyms=atpB {ECO:0000255|HAMAP-Rule:MF_01347}; OrderedLocusNames=all5039;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2878921; DOI=10.1128/jb.169.1.80-86.1987;
RA Curtis S.E.;
RT "Genes encoding the beta and epsilon subunits of the proton-translocating
RT ATPase from Anabaena sp. strain PCC 7120.";
RL J. Bacteriol. 169:80-86(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(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 four main
CC subunits: a(1), b(1), b'(1) and c(9-12). {ECO:0000255|HAMAP-
CC Rule:MF_01347}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01347}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC 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; M15336; AAA21993.1; -; Genomic_DNA.
DR EMBL; BA000019; BAB76738.1; -; Genomic_DNA.
DR PIR; A26926; A26926.
DR PIR; AG2435; AG2435.
DR RefSeq; WP_010999165.1; NZ_RSCN01000014.1.
DR AlphaFoldDB; P06540; -.
DR SMR; P06540; -.
DR STRING; 103690.17134177; -.
DR EnsemblBacteria; BAB76738; BAB76738; BAB76738.
DR KEGG; ana:all5039; -.
DR eggNOG; COG0055; Bacteria.
DR OMA; GFNMIMD; -.
DR OrthoDB; 430176at2; -.
DR Proteomes; UP000002483; Chromosome.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid 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; CF(1); Hydrogen ion transport; Ion transport;
KW Membrane; Nucleotide-binding; Reference proteome; Thylakoid; Translocase;
KW Transport.
FT CHAIN 1..482
FT /note="ATP synthase subunit beta"
FT /id="PRO_0000144414"
FT BINDING 162..169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
FT CONFLICT 208..222
FT /note="ESGVINNENLNESKI -> DSKN (in Ref. 1; AAA21993)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="I -> L (in Ref. 1; AAA21993)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 482 AA; 52016 MW; 976CD89D627D60D9 CRC64;
MVTTAEKTNI GYITQIIGPV VDVKFPNGKL PQIYNALTIK GTNEAGQQLN LTVEVQQLLG
DNQIRAVAMS STDGLVRGLE VVDTGAPISV PVGKATLGRI FNVLGEPVDN RGPVNNQETL
PIHRPAPKLT ELETKPSVFE TGIKVVDLLT PYRRGGKIGL FGGAGVGKTV IMMELINNIA
TQHGGVSVFA GVGERTREGN DLYNEMIESG VINNENLNES KIALVYGQMN EPPGARMRVG
LSGLTMAEYF RDVNKQDVLL FIDNIFRFVQ AGSEVSALLG RMPSAVGYQP TLGTDVGQLQ
ERITSTTEGS ITSIQAVYVP ADDLTDPAPA TTFAHLDGTT VLSRGLASKG IYPAVDPLGS
TSTMLQPNIV GDEHYNTARA VQSTLQRYKE LQDIIAILGL DELSEEDRLI VARARKVERF
LSQPFFVAEV FTGSPGKYVK LEDTIKGFQK ILSGELDDLP EQAFYLVGDI NEAIAKAEKI
KG
