ID   ATPF2_BRADU             Reviewed;         187 AA.
AC   Q89V70;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=ATP synthase subunit b 2;
DE   AltName: Full=ATP synthase F(0) sector subunit b 2;
DE   AltName: Full=ATPase subunit I 2;
DE   AltName: Full=F-type ATPase subunit b 2;
DE            Short=F-ATPase subunit b 2;
GN   Name=atpF2; Synonyms=atpG; OrderedLocusNames=bll1186;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- FUNCTION: Component of the F(0) channel, it forms part of the
CC       peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged
CC       and duplicated form of b found in plants and photosynthetic bacteria
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core
CC       - and F(0) - the membrane proton channel. F(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main
CC       subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an
CC       alternating ring which encloses part of the gamma chain. F(1) is
CC       attached to F(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       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATPase B chain family. {ECO:0000305}.
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DR   EMBL; BA000040; BAC46451.1; -; Genomic_DNA.
DR   RefSeq; NP_767826.1; NC_004463.1.
DR   RefSeq; WP_011084005.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89V70; -.
DR   SMR; Q89V70; -.
DR   STRING; 224911.27349437; -.
DR   EnsemblBacteria; BAC46451; BAC46451; BAC46451.
DR   GeneID; 64021056; -.
DR   KEGG; bja:bll1186; -.
DR   PATRIC; fig|224911.44.peg.589; -.
DR   eggNOG; COG0711; Bacteria.
DR   HOGENOM; CLU_079215_1_2_5; -.
DR   InParanoid; Q89V70; -.
DR   OMA; NQIFWLV; -.
DR   PhylomeDB; Q89V70; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01398; ATP_synth_b_bprime; 1.
DR   InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR   Pfam; PF00430; ATP-synt_B; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Cell inner membrane; Cell membrane; CF(0);
KW   Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..187
FT                   /note="ATP synthase subunit b 2"
FT                   /id="PRO_0000369002"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          103..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   187 AA;  18973 MW;  C2006A5746E79AF2 CRC64;
     MAESHGGAKG PAAGAHTGAE GGHGGGFPPF ESSTYASQLV SLAIFFVVLY VIVSKLALPK
     VGGAIEARQN KIEGDLAEAQ TLRDQSDAAL KAYESELASA RSRAQAIGNE SRDKANAQAE
     TERKALEEQL AAKLAGAEKT IASTRTAAMS NVRGIAADAA GQIVQQLTGV VPDAASVNAA
     VDASLKG