ID   ATPF2_PROMA             Reviewed;         153 AA.
AC   Q7VA60;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=ATP synthase subunit b' {ECO:0000255|HAMAP-Rule:MF_01399};
DE   AltName: Full=ATP synthase F(0) sector subunit b' {ECO:0000255|HAMAP-Rule:MF_01399};
DE   AltName: Full=ATPase subunit II {ECO:0000255|HAMAP-Rule:MF_01399};
DE   AltName: Full=F-type ATPase subunit b' {ECO:0000255|HAMAP-Rule:MF_01399};
DE            Short=F-ATPase subunit b' {ECO:0000255|HAMAP-Rule:MF_01399};
GN   Name=atpF2 {ECO:0000255|HAMAP-Rule:MF_01399};
GN   Synonyms=atpG {ECO:0000255|HAMAP-Rule:MF_01399};
GN   OrderedLocusNames=Pro_1607;
OS   Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARG / CCMP1375 / SS120;
RX   PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA   Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA   Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA   Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA   Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT   "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT   nearly minimal oxyphototrophic genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
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_01399}.
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       {ECO:0000255|HAMAP-Rule:MF_01399}.
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 four main
CC       subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains
CC       form an alternating ring which encloses part of the gamma chain. F(1)
CC       is 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, b and b'
CC       chains. {ECO:0000255|HAMAP-Rule:MF_01399}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01399}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01399}.
CC   -!- SIMILARITY: Belongs to the ATPase B chain family. {ECO:0000255|HAMAP-
CC       Rule:MF_01399}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE017126; AAQ00651.1; -; Genomic_DNA.
DR   RefSeq; NP_875998.1; NC_005042.1.
DR   RefSeq; WP_011125757.1; NC_005042.1.
DR   AlphaFoldDB; Q7VA60; -.
DR   SMR; Q7VA60; -.
DR   STRING; 167539.Pro_1607; -.
DR   EnsemblBacteria; AAQ00651; AAQ00651; Pro_1607.
DR   GeneID; 54200931; -.
DR   KEGG; pma:Pro_1607; -.
DR   PATRIC; fig|167539.5.peg.1698; -.
DR   eggNOG; COG0711; Bacteria.
DR   HOGENOM; CLU_079215_9_0_3; -.
DR   OMA; PLMAIQF; -.
DR   OrthoDB; 1999641at2; -.
DR   Proteomes; UP000001420; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid 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   HAMAP; MF_01399; ATP_synth_bprime; 1.
DR   InterPro; IPR034679; ATP_synth_b.
DR   InterPro; IPR028987; ATP_synth_B-like_membr_sf.
DR   InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR   Pfam; PF00430; ATP-synt_B; 1.
DR   SUPFAM; SSF81573; SSF81573; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW   Reference proteome; Thylakoid; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..153
FT                   /note="ATP synthase subunit b'"
FT                   /id="PRO_0000369020"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01399"
SQ   SEQUENCE   153 AA;  17056 MW;  78A09B52E141E7E5 CRC64;
     MTSLLLFGAS EGGLFDFDAT LPLMAAQVVL LTFILNALFF KPVGRVVEDR EDYVLTSRAE
     AKKKLAEVEK LENDLKNQLK EARKAAQQVI SEAEEDSEKL YKEALNLANS EANASREQAR
     REIDSQRDSA LKKLKSDSDK LGDLIVERLL AAK