ID   ATPF2_BRUO2             Reviewed;         159 AA.
AC   A5VNW5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=ATP synthase subunit b 2 {ECO:0000255|HAMAP-Rule:MF_01398};
DE   AltName: Full=ATP synthase F(0) sector subunit b 2 {ECO:0000255|HAMAP-Rule:MF_01398};
DE   AltName: Full=ATPase subunit I 2 {ECO:0000255|HAMAP-Rule:MF_01398};
DE   AltName: Full=F-type ATPase subunit b 2 {ECO:0000255|HAMAP-Rule:MF_01398};
DE            Short=F-ATPase subunit b 2 {ECO:0000255|HAMAP-Rule:MF_01398};
GN   Name=atpF2 {ECO:0000255|HAMAP-Rule:MF_01398}; OrderedLocusNames=BOV_0397;
OS   Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=444178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25840 / 63/290 / NCTC 10512;
RX   PubMed=19436743; DOI=10.1371/journal.pone.0005519;
RA   Tsolis R.M., Seshadri R., Santos R.L., Sangari F.J., Lobo J.M.,
RA   de Jong M.F., Ren Q., Myers G., Brinkac L.M., Nelson W.C., Deboy R.T.,
RA   Angiuoli S., Khouri H., Dimitrov G., Robinson J.R., Mulligan S.,
RA   Walker R.L., Elzer P.E., Hassan K.A., Paulsen I.T.;
RT   "Genome degradation in Brucella ovis corresponds with narrowing of its host
RT   range and tissue tropism.";
RL   PLoS ONE 4:E5519-E5519(2009).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_01398}.
CC   -!- FUNCTION: Component of the F(0) channel, it forms part of the
CC       peripheral stalk, linking F(1) to F(0). {ECO:0000255|HAMAP-
CC       Rule:MF_01398}.
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       {ECO:0000255|HAMAP-Rule:MF_01398}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01398}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01398}.
CC   -!- SIMILARITY: Belongs to the ATPase B chain family. {ECO:0000255|HAMAP-
CC       Rule:MF_01398}.
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DR   EMBL; CP000708; ABQ60781.1; -; Genomic_DNA.
DR   RefSeq; WP_005978305.1; NC_009505.1.
DR   AlphaFoldDB; A5VNW5; -.
DR   SMR; A5VNW5; -.
DR   EnsemblBacteria; ABQ60781; ABQ60781; BOV_0397.
DR   GeneID; 45123878; -.
DR   KEGG; bov:BOV_0397; -.
DR   HOGENOM; CLU_079215_6_1_5; -.
DR   OMA; KVPGMMA; -.
DR   PhylomeDB; A5VNW5; -.
DR   Proteomes; UP000006383; Chromosome I.
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   InterPro; IPR005864; ATP_synth_F0_bsu_bac.
DR   Pfam; PF00430; ATP-synt_B; 1.
DR   TIGRFAMs; TIGR01144; 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; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..159
FT                   /note="ATP synthase subunit b 2"
FT                   /id="PRO_0000368373"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
SQ   SEQUENCE   159 AA;  17441 MW;  68FF2AE85B4E8211 CRC64;
     MDATFWAFIA LVIFVAIVVY MKVPGMIGRT LDERADRIKK ELEEARTLRE EAQQLLAEYH
     RKCKEAEKEA GDIVASAERE AKALLEEAKR ATEEYVARRN KLAEQKIATA ETDAINAVRA
     SAVDLAVAAA GSILAEKVDA KAAGNLFNDA LAQVKSHLN