ID   ATPF2_PROM3             Reviewed;         151 AA.
AC   A2C6X2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=P9303_04801;
OS   Prochlorococcus marinus (strain MIT 9303).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9303;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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}.
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DR   EMBL; CP000554; ABM77232.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2C6X2; -.
DR   SMR; A2C6X2; -.
DR   STRING; 59922.P9303_04801; -.
DR   EnsemblBacteria; ABM77232; ABM77232; P9303_04801.
DR   KEGG; pmf:P9303_04801; -.
DR   HOGENOM; CLU_079215_9_0_3; -.
DR   OMA; PLMAIQF; -.
DR   BioCyc; PMAR59922:G1G80-442-MON; -.
DR   Proteomes; UP000002274; 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   Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..151
FT                   /note="ATP synthase subunit b'"
FT                   /id="PRO_0000369025"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01399"
SQ   SEQUENCE   151 AA;  16742 MW;  7D14E19ECB4DE9CF CRC64;
     MTSLLLFGAG GLFDFDATLP LMALQVVLLT FILNALFFRP VGRVVEEREV YVTTSRAEAK
     QKLAEAEKLE LELKEQLKSA RIAAQQLIQE AEKDSEQLYR EALAIANADA NAAREKARRE
     IDAQRDSALT QLKGDAEKLG DLIVNRLLAA K