ID   ATPF_SYNPW              Reviewed;         171 AA.
AC   A5GND0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=ATP synthase subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
DE   AltName: Full=ATP synthase F(0) sector subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
DE   AltName: Full=ATPase subunit I {ECO:0000255|HAMAP-Rule:MF_01398};
DE   AltName: Full=F-type ATPase subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
DE            Short=F-ATPase subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
GN   Name=atpF {ECO:0000255|HAMAP-Rule:MF_01398};
GN   OrderedLocusNames=SynWH7803_2019;
OS   Synechococcus sp. (strain WH7803).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=32051;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH7803;
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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 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_01398}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid 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; CT971583; CAK24445.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5GND0; -.
DR   SMR; A5GND0; -.
DR   STRING; 32051.SynWH7803_2019; -.
DR   PRIDE; A5GND0; -.
DR   EnsemblBacteria; CAK24445; CAK24445; SynWH7803_2019.
DR   KEGG; syx:SynWH7803_2019; -.
DR   eggNOG; COG0711; Bacteria.
DR   HOGENOM; CLU_079215_8_1_3; -.
DR   OMA; NILNWAV; -.
DR   Proteomes; UP000001566; 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   InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR   Pfam; PF00430; ATP-synt_B; 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..171
FT                   /note="ATP synthase subunit b"
FT                   /id="PRO_0000368832"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
SQ   SEQUENCE   171 AA;  18716 MW;  53FD6B39357E9B64 CRC64;
     MPLPLFASEG GFGLNLNLFE TNLINLVIVI GVLYWFLKGF LGGILERRRQ AILKDLEDSE
     GRLRQATTDL ARAQEDLAAA QQKAEKIRSD GKARAEAIRK DGEMRTINAM AAVKQDALAD
     LNAEGARLTE QLRREAALAA IDKVMTELPG RLDQAGQSRL IDASISNLED A