ATPF_PELUB
ID ATPF_PELUB Reviewed; 179 AA.
AC Q4FPE7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=ATP synthase subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=ATP synthase F(0) sector subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=ATPase subunit I {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=F-type ATPase subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
DE Short=F-ATPase subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
GN Name=atpF {ECO:0000255|HAMAP-Rule:MF_01398}; OrderedLocusNames=SAR11_0118;
OS Pelagibacter ubique (strain HTCC1062).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Pelagibacterales;
OC Pelagibacteraceae; Candidatus Pelagibacter.
OX NCBI_TaxID=335992;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC1062;
RX PubMed=16109880; DOI=10.1126/science.1114057;
RA Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L., Baptista D.,
RA Bibbs L., Eads J., Richardson T.H., Noordewier M., Rappe M.S., Short J.M.,
RA Carrington J.C., Mathur E.J.;
RT "Genome streamlining in a cosmopolitan oceanic bacterium.";
RL Science 309:1242-1245(2005).
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_01398}.
CC -!- FUNCTION: Component of the F(0) channel, it forms part of the
CC peripheral stalk, linking F(1) to F(0). {ECO:0000255|HAMAP-
CC Rule:MF_01398}.
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 three main
CC subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an
CC alternating ring which encloses part of the gamma chain. F(1) is
CC 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 and b chains.
CC {ECO:0000255|HAMAP-Rule:MF_01398}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01398}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01398}.
CC -!- SIMILARITY: Belongs to the ATPase B chain family. {ECO:0000255|HAMAP-
CC Rule:MF_01398}.
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DR EMBL; CP000084; AAZ20942.1; -; Genomic_DNA.
DR RefSeq; WP_011281483.1; NC_007205.1.
DR AlphaFoldDB; Q4FPE7; -.
DR SMR; Q4FPE7; -.
DR STRING; 335992.SAR11_0118; -.
DR PRIDE; Q4FPE7; -.
DR EnsemblBacteria; AAZ20942; AAZ20942; SAR11_0118.
DR GeneID; 66294621; -.
DR KEGG; pub:SAR11_0118; -.
DR eggNOG; COG0711; Bacteria.
DR HOGENOM; CLU_079215_1_2_5; -.
DR OMA; NQIFWLV; -.
DR OrthoDB; 1544382at2; -.
DR Proteomes; UP000002528; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma 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 InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR Pfam; PF00430; ATP-synt_B; 1.
PE 3: Inferred from homology;
KW ATP synthesis; Cell inner membrane; Cell membrane; CF(0);
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..179
FT /note="ATP synthase subunit b"
FT /id="PRO_0000368647"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
SQ SEQUENCE 179 AA; 20558 MW; 904293F1A2C42009 CRC64;
MEAFAAESGG MPQLNPEFWV SQIFWLIITF GILYVVLSKL ILPKISANLE NRKSQILENI
EAAEKQREES EQKIEEYEKI VQSSKNEAKN YFKQAREKVL KDIGVKREIL EKELDEEVNK
AEIEIKTFRD NAPEKIKKIA VETSSDLLQE LIGAEVNSSS ISAIVEDLSR KKMDEYYGN
