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Database: UniProt
Entry: A0A098G6Z6_9GAMM
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Original site: A0A098G6Z6_9GAMM 
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
//
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