ID A0A1Q8Z570_9CYAN Unreviewed; 143 AA.
AC A0A1Q8Z570;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=BST81_26770 {ECO:0000313|EMBL:OLP15369.1};
OS Leptolyngbya sp. 'hensonii'.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya group; Leptolyngbya.
OX NCBI_TaxID=1922337 {ECO:0000313|EMBL:OLP15369.1, ECO:0000313|Proteomes:UP000186296};
RN [1] {ECO:0000313|EMBL:OLP15369.1, ECO:0000313|Proteomes:UP000186296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=hensonii {ECO:0000313|Proteomes:UP000186296};
RA Hamilton T.L., Klatt J.M., De Beer D., Macalady J.;
RT "Physiology of photosynthesis in the novel isolate Oscillatoriales
RT cyanobacterium hensonii.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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:OLP15369.1}.
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DR EMBL; MQTZ01000076; OLP15369.1; -; Genomic_DNA.
DR RefSeq; WP_075601535.1; NZ_MQTZ01000076.1.
DR AlphaFoldDB; A0A1Q8Z570; -.
DR STRING; 1922337.BST81_26770; -.
DR OrthoDB; 426571at2; -.
DR Proteomes; UP000186296; 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; 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.
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 Reference proteome {ECO:0000313|Proteomes:UP000186296};
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 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01399"
FT COILED 45..116
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 143 AA; 16206 MW; C1EC7F2544DD4D00 CRC64;
MFDFNATLPL MAIQFLLLAA VLNILFYKPL TKVLDERNEY IRKNETEARE RLAKAEQLAK
QYEQELAETR KQYQATIASA QADADKVAAQ QVAEAQREAQ AQREQVQREI DTQKQAALTS
LEGQVDNLSR QILEKLLGAE LVG
//
