ID A0A098G6Z6_9GAMM Unreviewed; 247 AA.
AC A0A098G6Z6;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=ATP synthase subunit b {ECO:0000313|EMBL:CEG57754.1};
GN Name=atpF {ECO:0000313|EMBL:CEG57754.1};
GN ORFNames=LFA_2383 {ECO:0000313|EMBL:CEG57754.1};
OS Legionella fallonii LLAP-10.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1212491 {ECO:0000313|EMBL:CEG57754.1, ECO:0000313|Proteomes:UP000032430};
RN [1] {ECO:0000313|Proteomes:UP000032430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC700992 {ECO:0000313|Proteomes:UP000032430};
RA Gomez-Valero L.;
RL Submitted (SEP-2014) 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|ARBA:ARBA00025614}.
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}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the ATPase B chain family.
CC {ECO:0000256|ARBA:ARBA00005513, ECO:0000256|RuleBase:RU003848}.
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DR EMBL; LN614827; CEG57754.1; -; Genomic_DNA.
DR RefSeq; WP_045096195.1; NZ_LN614827.1.
DR AlphaFoldDB; A0A098G6Z6; -.
DR STRING; 1212491.LFA_2383; -.
DR KEGG; lfa:LFA_2383; -.
DR HOGENOM; CLU_070737_1_0_6; -.
DR OrthoDB; 466272at2; -.
DR Proteomes; UP000032430; Chromosome.
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:InterPro.
DR CDD; cd06503; ATP-synt_Fo_b; 1.
DR InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR InterPro; IPR000711; ATPase_OSCP/dsu.
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 Pfam; PF00213; OSCP; 1.
DR PRINTS; PR00125; ATPASEDELTA.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310};
KW CF(0) {ECO:0000256|ARBA:ARBA00022547, ECO:0000256|RuleBase:RU003848};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW ECO:0000256|RuleBase:RU003848};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU003848};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000032430};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003848};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003848}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT COILED 59..86
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 247 AA; 28934 MW; 7E825BACC02CCC36 CRC64;
MELSWSTLIL EIINFLVLIW ILNYFLYAPI QKTIIARKKM VADKLEHAET LRSESQDLQL
KYENRLADWQ VEKERLQKEF QLKLEQWKSA EVVDFEKKLA TEKEALLVRE MKKSKELIEK
NAREAMLLAG KFSVKFLKNF ADEHLEEKII EKTILDLEDL PVEKIQFLTS QSSQDTILIQ
SAYPINEQQR HILVETIEKL SHKQFKVDFS VTPELLAGLM IQIGSVVLQA NLRDELKFFT
EIKNAIA
//