ID   ATPF_MYCGE              Reviewed;         208 AA.
AC   P47643;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   10-JUN-2026, entry version 147.
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};
DE   Flags: Precursor;
GN   Name=atpF {ECO:0000255|HAMAP-Rule:MF_01398}; OrderedLocusNames=MG403;
OS   Mycoplasmoides genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 /
OS   G37) (Mycoplasma genitalium).
OC   Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Mycoplasmoides.
OX   NCBI_TaxID=243273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA   Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA   Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA   Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA   Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA   Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA   Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT   "The minimal gene complement of Mycoplasma genitalium.";
RL   Science 270:397-403(1995).
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 membrane {ECO:0000255|HAMAP-Rule:MF_01398};
CC       Single-pass membrane protein {ECO:0000255|HAMAP-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; L43967; AAC71631.1; -; Genomic_DNA.
DR   PIR; F64244; F64244.
DR   RefSeq; WP_009885620.1; NC_000908.2.
DR   AlphaFoldDB; P47643; -.
DR   SMR; P47643; -.
DR   FunCoup; P47643; 57.
DR   STRING; 243273.MG_403; -.
DR   GeneID; 99647309; -.
DR   KEGG; mge:MG_403; -.
DR   eggNOG; COG0711; Bacteria.
DR   HOGENOM; CLU_079215_4_3_14; -.
DR   InParanoid; P47643; -.
DR   OrthoDB; 399036at2; -.
DR   BioCyc; MGEN243273:G1GJ2-500-MONOMER; -.
DR   Proteomes; UP000000807; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045259; C:proton-transporting ATP synthase complex; IBA:GO_Central.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR   CDD; cd06503; ATP-synt_Fo_b; 1.
DR   Gene3D; 1.20.5.620; F1F0 ATP synthase subunit B, membrane domain; 1.
DR   HAMAP; MF_01398; ATP_synth_b_bprime; 1.
DR   InterPro; IPR028987; ATP_synth_B-like_membr_sf.
DR   InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR   InterPro; IPR005864; ATP_synth_F0_bsu_bac.
DR   InterPro; IPR050059; ATP_synthase_B_chain.
DR   NCBIfam; TIGR01144; ATP_synt_b; 1.
DR   NCBIfam; NF004873; PRK06231.1-3; 1.
DR   PANTHER; PTHR33445:SF1; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Cell membrane; CF(0); Hydrogen ion transport; Ion transport;
KW   Lipoprotein; Membrane; Palmitate; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000250"
FT   CHAIN           28..208
FT                   /note="ATP synthase subunit b"
FT                   /id="PRO_0000002631"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
FT   LIPID           28
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           28
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   208 AA;  24603 MW;  0AB6526A367F84E6 CRC64;
     MVKAKKLVFK WSLLVFSFFT LSLFLVSCTE NVREIKSSSV INELFPNFWV FITHLLAFFI
     LLTLMIFLFW KPTQRFLNNR KNLLEAQIKQ ANELEKQARN LLEESNQRHE KALIVSKEIV
     DQANYEALQL KSEIEKTANR QANLMIFQAR QEIEKERRSL KEQSIKESVE LAMLAAQELI
     LKKIDQKSDR EFIDKFIRDL EANETEDD
//