ID   ATPF2_RHIME             Reviewed;         204 AA.
AC   Q92RM6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 96.
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=R00837; ORFNames=SMc00869;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481430; DOI=10.1073/pnas.161294398;
RA   Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA   Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA   Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA   Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA   Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT   "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT   meliloti strain 1021.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
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; AL591688; CAC45409.1; -; Genomic_DNA.
DR   RefSeq; NP_384943.1; NC_003047.1.
DR   RefSeq; WP_010968855.1; NC_003047.1.
DR   AlphaFoldDB; Q92RM6; -.
DR   SMR; Q92RM6; -.
DR   STRING; 266834.SMc00869; -.
DR   PRIDE; Q92RM6; -.
DR   EnsemblBacteria; CAC45409; CAC45409; SMc00869.
DR   GeneID; 61602303; -.
DR   KEGG; sme:SMc00869; -.
DR   PATRIC; fig|266834.11.peg.2229; -.
DR   eggNOG; COG0711; Bacteria.
DR   HOGENOM; CLU_079215_1_2_5; -.
DR   OMA; NQIFWLV; -.
DR   Proteomes; UP000001976; 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); IEA:UniProtKB-KW.
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..204
FT                   /note="ATP synthase subunit b 2"
FT                   /id="PRO_0000369035"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          8..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   204 AA;  21038 MW;  1AADE8B14F1BC27A CRC64;
     MFVTAAYAQS STTEGAEAHD AAAAGEVHTE TGVAHEADHG AGVFPPFDTT HFASQLLWLA
     ITFGLFYLLM SKVIIPRIGG ILETRHDRIA QDLDEASRLK GEADAAIAAY EQELAGARAK
     GHSIADTARE AAKAKAKADR DGVEAGLAKK IAAAEARIAD IKSKALADVG AIAEETATAV
     VKQLIGGTVT KAEIAAAFKA SAGN