ID L8MWY7_9CYAN Unreviewed; 165 AA.
AC L8MWY7;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=ATP synthase subunit b' {ECO:0000256|HAMAP-Rule:MF_01399};
DE AltName: Full=ATP synthase F(0) sector subunit b' {ECO:0000256|HAMAP-Rule:MF_01399};
DE AltName: Full=ATPase subunit II {ECO:0000256|HAMAP-Rule:MF_01399};
DE AltName: Full=F-type ATPase subunit b' {ECO:0000256|HAMAP-Rule:MF_01399};
DE Short=F-ATPase subunit b' {ECO:0000256|HAMAP-Rule:MF_01399};
GN Name=atpF2 {ECO:0000256|HAMAP-Rule:MF_01399};
GN Synonyms=atpG {ECO:0000256|HAMAP-Rule:MF_01399};
GN ORFNames=Pse7429DRAFT_3670 {ECO:0000313|EMBL:ELS31289.1};
OS Pseudanabaena biceps PCC 7429.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pseudanabaenales;
OC Pseudanabaenaceae; Pseudanabaena.
OX NCBI_TaxID=927668 {ECO:0000313|EMBL:ELS31289.1, ECO:0000313|Proteomes:UP000011201};
RN [1] {ECO:0000313|EMBL:ELS31289.1, ECO:0000313|Proteomes:UP000011201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7429 {ECO:0000313|EMBL:ELS31289.1,
RC ECO:0000313|Proteomes:UP000011201};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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:0000256|HAMAP-Rule:MF_01399}.
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.
CC {ECO:0000256|ARBA:ARBA00025198, ECO:0000256|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:0000256|HAMAP-Rule:MF_01399}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000256|HAMAP-
CC Rule:MF_01399}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01399}. Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the ATPase B chain family.
CC {ECO:0000256|ARBA:ARBA00005513, ECO:0000256|HAMAP-Rule:MF_01399,
CC ECO:0000256|RuleBase:RU003848}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELS31289.1}.
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DR EMBL; ALWB01000187; ELS31289.1; -; Genomic_DNA.
DR RefSeq; WP_009628630.1; NZ_ALWB01000187.1.
DR AlphaFoldDB; L8MWY7; -.
DR PATRIC; fig|927668.3.peg.4075; -.
DR OrthoDB; 426571at2; -.
DR Proteomes; UP000011201; Unassembled WGS sequence.
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 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 PANTHER; PTHR33445:SF2; ATP SYNTHASE SUBUNIT B; 1.
DR PANTHER; PTHR33445; ATP SYNTHASE SUBUNIT B', CHLOROPLASTIC; 1.
DR Pfam; PF00430; ATP-synt_B; 1.
DR SUPFAM; SSF81573; F1F0 ATP synthase subunit B, membrane domain; 1.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP-
KW Rule:MF_01399};
KW CF(0) {ECO:0000256|ARBA:ARBA00022547, ECO:0000256|HAMAP-Rule:MF_01399};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP-
KW Rule:MF_01399};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW Rule:MF_01399};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01399};
KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01399};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01399};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01399};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01399}.
FT TRANSMEM 26..49
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01399"
FT COILED 67..138
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 165 AA; 18173 MW; C05E8B5FD7AC95F1 CRC64;
MTIWNLFSTV LIAAEAAEHK GGLFDINATL PIMAVQFVVF VALLNVIFFK PLTKAIDDRD
DYVRGQIIGS KERLEKAELA VKQYEQELAS ARKATQNILT TAQAEANKIR KERIDAAMAE
AQAKVATAKA EIEKQKQDAT ASLDAEVESL SRQVLEKLLG NLVKS
//
