ATPF2_SYNR3
ID ATPF2_SYNR3 Reviewed; 155 AA.
AC A5GV75;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=SynRCC307_1881;
OS Synechococcus sp. (strain RCC307).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=316278;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC307;
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_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; CT978603; CAK28784.1; -; Genomic_DNA.
DR RefSeq; WP_011936297.1; NC_009482.1.
DR AlphaFoldDB; A5GV75; -.
DR SMR; A5GV75; -.
DR STRING; 316278.SynRCC307_1881; -.
DR EnsemblBacteria; CAK28784; CAK28784; SynRCC307_1881.
DR KEGG; syr:SynRCC307_1881; -.
DR eggNOG; COG0711; Bacteria.
DR HOGENOM; CLU_079215_9_0_3; -.
DR OMA; PLMAIQF; -.
DR OrthoDB; 1999641at2; -.
DR Proteomes; UP000001115; 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..155
FT /note="ATP synthase subunit b'"
FT /id="PRO_0000369055"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01399"
SQ SEQUENCE 155 AA; 16936 MW; DD3B9F5E88AFE0A6 CRC64;
MHSWLLLAEA ATPKGGLFDL DATLPLMAVQ VVVLTFVLNA LFFRPVGKTV EDREGYISTS
RAQAKEKLAQ AERLEAELKA QLLDARKQSV AVIQKAEEEV DRLFREALAV AQSEANSVRE
KARGEVDAEK AKAFSGIDSQ AEKLSSLIVD RLLAA
