ATPB_SYNP6
ID ATPB_SYNP6 Reviewed; 484 AA.
AC P07890;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 156.
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};
GN OrderedLocusNames=syc1787_c;
OS Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS nidulans).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=269084;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3041005; DOI=10.1016/0022-2836(87)90667-x;
RA Cozens A.L., Walker J.E.;
RT "The organization and sequence of the genes for ATP synthase subunits in
RT the cyanobacterium Synechococcus 6301. Support for an endosymbiotic origin
RT of chloroplasts.";
RL J. Mol. Biol. 194:359-383(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT Synechococcus elongatus PCC 6301 chromosome: gene content and
RT organization.";
RL Photosyn. Res. 93:55-67(2007).
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; X05925; CAA29362.1; -; Genomic_DNA.
DR EMBL; AP008231; BAD79977.1; -; Genomic_DNA.
DR PIR; S10837; PWYCB.
DR RefSeq; WP_011244097.1; NC_006576.1.
DR AlphaFoldDB; P07890; -.
DR SMR; P07890; -.
DR STRING; 269084.syc1787_c; -.
DR EnsemblBacteria; BAD79977; BAD79977; syc1787_c.
DR KEGG; syc:syc1787_c; -.
DR eggNOG; COG0055; Bacteria.
DR OMA; GFNMIMD; -.
DR Proteomes; UP000001175; 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; Thylakoid; Translocase; Transport.
FT CHAIN 1..484
FT /note="ATP synthase subunit beta"
FT /id="PRO_0000144482"
FT BINDING 162..169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ SEQUENCE 484 AA; 52213 MW; 2D53DCFE80C13FAA CRC64;
MVTTTEKTNI GYIRQVIGPV VDVEFPAGKL PQIYNALVIK GKNEAGQDLS VTCEVQQLLG
DRKVRAVSMS TTDGLVRGLE VIDTGAPISV PVGEATLGRI FNVLGEPVDE LGPVNAATTS
PIHRDAPKLT DLETKPKVFE TGIKVIDLLA PYRQGGKIGL FGGAGVGKTV LIQELINNIA
KEHGGVSVFG GVGERTREGN DLYQEFKESG VIDEKNIANS KVALVYGQMN EPPGARMRVG
LSALTMAEHF RDVNKQDVLL FIDNIFRFVQ AGSEVSALLG RMPSAVGYQP TLGTDVGQLQ
ERITSTLEGS ITSIQAVYVP ADDLTDPAPA TTFAHLDATT VLSRGLASKG IYPAVDPLDS
TSTMLQPSIV GEEHYRTARA VQSTLQRYKE LQDIIAILGL DELSEEDRQT VARARKIEKF
LSQPFFVAEV FTGSPGKYVK LEDTISGFNR ILNGELDDLP EQAFYLVGDI QEAIEKGAKL
KAES
