ID   ATPF2_SYNY3             Reviewed;         143 AA.
AC   P27183;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   04-NOV-2026, entry version 149.
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=sll1323;
OS   Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Merismopediaceae; Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1832989; DOI=10.1007/bf00037050;
RA   Lill H., Nelson N.;
RT   "The atp1 and atp2 operons of the cyanobacterium Synechocystis sp. PCC
RT   6803.";
RL   Plant Mol. Biol. 17:641-652(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; X58128; CAA41132.1; -; Genomic_DNA.
DR   EMBL; BA000022; BAA16738.1; -; Genomic_DNA.
DR   PIR; S17748; PWYBBI.
DR   SMR; P27183; -.
DR   IntAct; P27183; 8.
DR   STRING; 1148.gene:10497593; -.
DR   PaxDb; 1148-gene:10497593; -.
DR   EnsemblBacteria; BAA16738; BAA16738; BAA16738.
DR   KEGG; syn:sll1323; -.
DR   eggNOG; COG0711; Bacteria.
DR   InParanoid; P27183; -.
DR   OMA; AFMFLMY; -.
DR   PhylomeDB; P27183; -.
DR   CDD; cd06503; ATP-synt_Fo_b; 1.
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   InterPro; IPR050059; ATP_synthase_B_chain.
DR   PANTHER; PTHR33445; ATP SYNTHASE SUBUNIT B', CHLOROPLASTIC; 1.
DR   PANTHER; PTHR33445:SF2; ATP SYNTHASE SUBUNIT B', CHLOROPLASTIC; 1.
DR   Pfam; PF00430; ATP-synt_B; 1.
DR   SUPFAM; SSF81573; F1F0 ATP synthase subunit B, membrane domain; 1.
DR   NCBIfam; NF005607; PRK07353.1; 1.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045259; C:proton-transporting ATP synthase complex; IDA:UniProtKB.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR   Proteomes; UP000001425; Chromosome.
DR   AlphaFoldDB; P27183; -.
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..143
FT                   /note="ATP synthase subunit b'"
FT                   /id="PRO_0000082430"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01399"
SQ   SEQUENCE   143 AA;  16245 MW;  A46B75F5B64A02CC CRC64;
     MFDFDATLPL MALQFVVLAF LLNAIFYKPM NKVLDERADY IRTNEEDARE RLAKAKAITQ
     EYEQQITDAR RQSQAVIADA QAEARRLAAE KIAEAQRESQ RQKETAAQEI EAQRQSALSS
     LEQEVAALSN QILHKLLGPE LIK
//