ATPB_ANTAG
ID ATPB_ANTAG Reviewed; 492 AA.
AC Q31794; O49837; Q85UU1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=ATP synthase subunit beta, chloroplastic {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=atpB {ECO:0000255|HAMAP-Rule:MF_01347};
OS Anthoceros angustus (Hornwort) (Anthoceros formosae).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Anthocerotophyta;
OC Anthocerotopsida; Anthocerotidae; Anthocerotales; Anthocerotaceae;
OC Anthoceros.
OX NCBI_TaxID=48387;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND RNA EDITING.
RC TISSUE=Thallus;
RX PubMed=8604330; DOI=10.1093/nar/24.6.1008;
RA Yoshinaga K., Iinuma H., Masuzawa T., Ueda K.;
RT "Extensive RNA editing of U to C in addition to C to U substitution in the
RT rbcL transcripts of hornwort chloroplasts and the origin of RNA editing in
RT green plants.";
RL Nucleic Acids Res. 24:1008-1014(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND RNA EDITING.
RX PubMed=9365264; DOI=10.1093/nar/25.23.4830;
RA Yoshinaga K., Kakehi T., Shima Y., Iinuma H., Masuzawa T., Ueno M.;
RT "Extensive RNA editing and possible double-stranded structures determining
RT editing sites in the atpB transcripts of hornwort chloroplasts.";
RL Nucleic Acids Res. 25:4830-4834(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING.
RX PubMed=12527781; DOI=10.1093/nar/gkg155;
RA Kugita M., Kaneko A., Yamamoto Y., Takeya Y., Matsumoto T., Yoshinaga K.;
RT "The complete nucleotide sequence of the hornwort (Anthoceros formosae)
RT chloroplast genome: insight into the earliest land plants.";
RL Nucleic Acids Res. 31:716-721(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND RNA EDITING.
RC TISSUE=Thallus;
RX PubMed=12711687; DOI=10.1093/nar/gkg327;
RA Kugita M., Yamamoto Y., Fujikawa T., Matsumoto T., Yoshinaga K.;
RT "RNA editing in hornwort chloroplasts makes more than half the genes
RT functional.";
RL Nucleic Acids Res. 31:2417-2423(2003).
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: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01347}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01347}.
CC -!- RNA EDITING: Modified_positions=1 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687, ECO:0000269|PubMed:8604330,
CC ECO:0000269|PubMed:9365264}, 65 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687, ECO:0000269|PubMed:8604330,
CC ECO:0000269|PubMed:9365264}, 139 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687, ECO:0000269|PubMed:8604330,
CC ECO:0000269|PubMed:9365264}, 159 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687, ECO:0000269|PubMed:8604330,
CC ECO:0000269|PubMed:9365264}, 162 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687, ECO:0000269|PubMed:8604330,
CC ECO:0000269|PubMed:9365264}, 168 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687, ECO:0000269|PubMed:8604330,
CC ECO:0000269|PubMed:9365264}, 249 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687, ECO:0000269|PubMed:8604330,
CC ECO:0000269|PubMed:9365264}, 251 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687, ECO:0000269|PubMed:8604330,
CC ECO:0000269|PubMed:9365264}, 267 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687, ECO:0000269|PubMed:8604330,
CC ECO:0000269|PubMed:9365264}, 274 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687, ECO:0000269|PubMed:8604330,
CC ECO:0000269|PubMed:9365264}, 275 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687, ECO:0000269|PubMed:8604330,
CC ECO:0000269|PubMed:9365264}, 286 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687, ECO:0000269|PubMed:8604330,
CC ECO:0000269|PubMed:9365264}, 287 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687, ECO:0000269|PubMed:8604330,
CC ECO:0000269|PubMed:9365264}, 313 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687, ECO:0000269|PubMed:8604330,
CC ECO:0000269|PubMed:9365264}, 329 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687, ECO:0000269|PubMed:8604330,
CC ECO:0000269|PubMed:9365264}, 335 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687, ECO:0000269|PubMed:8604330,
CC ECO:0000269|PubMed:9365264}, 344 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687, ECO:0000269|PubMed:8604330,
CC ECO:0000269|PubMed:9365264}, 351 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687, ECO:0000269|PubMed:8604330,
CC ECO:0000269|PubMed:9365264}, 361 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687, ECO:0000269|PubMed:8604330,
CC ECO:0000269|PubMed:9365264}, 362 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687, ECO:0000269|PubMed:8604330,
CC ECO:0000269|PubMed:9365264}, 370 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687, ECO:0000269|PubMed:8604330,
CC ECO:0000269|PubMed:9365264}, 405 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687, ECO:0000269|PubMed:8604330,
CC ECO:0000269|PubMed:9365264}, 408 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687, ECO:0000269|PubMed:8604330,
CC ECO:0000269|PubMed:9365264}, 411 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687, ECO:0000269|PubMed:8604330,
CC ECO:0000269|PubMed:9365264}, 439 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687, ECO:0000269|PubMed:8604330,
CC ECO:0000269|PubMed:9365264}, 470 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687, ECO:0000269|PubMed:8604330,
CC ECO:0000269|PubMed:9365264}, 472 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687, ECO:0000269|PubMed:8604330,
CC ECO:0000269|PubMed:9365264}, 478 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687, ECO:0000269|PubMed:8604330,
CC ECO:0000269|PubMed:9365264}; Note=The initiator methionine is created
CC by editing. The nonsense codons at positions 65, 139 and 470 are
CC modified to sense codons.;
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01347}.
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DR EMBL; D86545; BAA24160.1; -; mRNA.
DR EMBL; D43695; BAA07795.1; -; Genomic_DNA.
DR EMBL; AB086179; BAC55356.1; -; Genomic_DNA.
DR EMBL; AB087448; BAC55452.1; -; mRNA.
DR EMBL; AB087447; BAC55451.1; -; mRNA.
DR PIR; S71146; S71146.
DR RefSeq; NP_777420.1; NC_004543.1.
DR AlphaFoldDB; Q31794; -.
DR SMR; Q31794; -.
DR GeneID; 2553481; -.
DR GO; GO:0009535; C:chloroplast 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 2: Evidence at transcript level;
KW ATP synthesis; ATP-binding; CF(1); Chloroplast; Hydrogen ion transport;
KW Ion transport; Membrane; Nucleotide-binding; Plastid; RNA editing;
KW Thylakoid; Translocase; Transport.
FT CHAIN 1..492
FT /note="ATP synthase subunit beta, chloroplastic"
FT /id="PRO_0000144495"
FT BINDING 170..177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ SEQUENCE 492 AA; 53161 MW; 5813D54D8C483223 CRC64;
MKTNYLILGV STLISKNVGH ISQIIGPVLD VTFPPGKMPN IYNSLIVRGQ NPAGQEINVT
CEVQQLLGNN KVRAVAMSAT DGLTRGMKVT DTGAPLSVPV GEVTLGRIFN VLGEPVDNLG
AIDVSTTFPI HRSAPAFTQL DTKLSIFETG IKVVDLLAPY RRGGKIGLFG GAGVGKTVLI
MELINNIAKA HGGVSVFGGV GERTREGNDL YMEMKESKVI NEQDISESKV ALVYGQMNEP
PGARMRVGLT ALTMAEYFRD VNKQDVLLFI DNIFRFVQAG SEVSALLGRM PSAVGYQPTL
STEMGSLQER ITSTKEGSIT SIQAVYVPAD DLTDPAPATT FAHLDATTVL SRGLAAKGIY
PAVDPLDSTS TMLQPWIVGE EHYETAQGVK QTLQRYKELQ DIIAILGLDE LSEEDRLTVA
RARKIERFLS QPFFVAEVFT GSPGKYVSLI ETIKGFQMIL AGELDGLPEQ AFYLVGNIDE
VTAKAETLQM ES
