ID G7JAI2_MEDTR Unreviewed; 209 AA.
AC G7JAI2;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=ATP synthase, F0 subunit B {ECO:0000313|EMBL:AES73621.1};
DE SubName: Full=Putative ATP synthase, F0 complex, subunit B/B' protein {ECO:0000313|EMBL:RHN70623.1};
GN Name=11432459 {ECO:0000313|EnsemblPlants:AES73621};
GN OrderedLocusNames=MTR_3g106820 {ECO:0000313|EMBL:AES73621.1};
GN ORFNames=MtrunA17_Chr3g0137561 {ECO:0000313|EMBL:RHN70623.1};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880 {ECO:0000313|EMBL:AES73621.1, ECO:0000313|Proteomes:UP000002051};
RN [1] {ECO:0000313|EMBL:AES73621.1, ECO:0000313|Proteomes:UP000002051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A17 {ECO:0000313|EMBL:AES73621.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:AES73621,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [2] {ECO:0000313|EMBL:AFK46888.1}
RP NUCLEOTIDE SEQUENCE.
RA Krishnakumar V., Cheung F., Xiao Y., Chan A., Moskal W.A., Town C.D.;
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AES73621.1, ECO:0000313|Proteomes:UP000002051}
RP GENOME REANNOTATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES73621,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [4] {ECO:0000313|EnsemblPlants:AES73621}
RP IDENTIFICATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES73621};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
RN [5] {ECO:0000313|EMBL:RHN70623.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:RHN70623.1};
RA Pecrix Y., Gamas P., Carrere S.;
RT "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL Nat. Plants 0:0-0(2018).
CC -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence
CC of a proton or sodium gradient. F-type ATPases consist of two
CC structural domains, F(1) containing the extramembraneous catalytic core
CC and F(0) containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation.
CC {ECO:0000256|ARBA:ARBA00025198}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the ATPase B chain family.
CC {ECO:0000256|ARBA:ARBA00005513, ECO:0000256|RuleBase:RU003848}.
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DR EMBL; CM001219; AES73621.1; -; Genomic_DNA.
DR EMBL; BT147094; AFK46888.1; -; mRNA.
DR EMBL; PSQE01000003; RHN70623.1; -; Genomic_DNA.
DR RefSeq; XP_003603370.1; XM_003603322.2.
DR AlphaFoldDB; G7JAI2; -.
DR STRING; 3880.G7JAI2; -.
DR PaxDb; 3880-AES73621; -.
DR ProMEX; G7JAI2; -.
DR EnsemblPlants; AES73621; AES73621; MTR_3g106820.
DR GeneID; 11432459; -.
DR Gramene; AES73621; AES73621; MTR_3g106820.
DR KEGG; mtr:11432459; -.
DR eggNOG; ENOG502RH8G; Eukaryota.
DR HOGENOM; CLU_079215_0_1_1; -.
DR OMA; PLMAIQF; -.
DR OrthoDB; 314390at2759; -.
DR Proteomes; UP000002051; Chromosome 3.
DR Proteomes; UP000265566; Chromosome 3.
DR ExpressionAtlas; G7JAI2; differential.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
DR CDD; cd06503; ATP-synt_Fo_b; 1.
DR HAMAP; MF_01398; ATP_synth_b_bprime; 1.
DR HAMAP; MF_01399; ATP_synth_bprime; 1.
DR InterPro; IPR034679; ATP_synth_b.
DR InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR PANTHER; PTHR33445:SF2; ATP SYNTHASE SUBUNIT B; 1.
DR PANTHER; PTHR33445; ATP SYNTHASE SUBUNIT B', CHLOROPLASTIC; 1.
DR Pfam; PF00430; ATP-synt_B; 1.
PE 2: Evidence at transcript level;
KW CF(0) {ECO:0000256|ARBA:ARBA00022547, ECO:0000256|RuleBase:RU003848};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW ECO:0000256|RuleBase:RU003848};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU003848}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000002051};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003848};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003848}.
FT COILED 109..199
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 209 AA; 23050 MW; 79C46D62273F496E CRC64;
MASMIMASSK PIIRVPTNSL PSTPKLPSLQ TITPNLKLQL SKLKSMTLAA TSLSFVFAPP
SLAFEKAALF DFNLTLPIIV VEFLFLMFAL DKLYFTPLGT FMDNRDAEIR GKLNSVTNTS
EEVKELEEQA NAVLRAARAE IAVALNQMKK ETQAEVEEKI AEGRKKVDAE LQEALANLEK
QKEETVKALD SQIAALSQDI VNKVLPVSR
//
