ID   ATPF_CORDI              Reviewed;         188 AA.
AC   Q6NHT3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   02-SEP-2026, entry version 113.
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};
GN   OrderedLocusNames=DIP1048;
OS   Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS   gravis).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=257309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis;
RX   PubMed=14602910; DOI=10.1093/nar/gkg874;
RA   Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G.,
RA   Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D.,
RA   De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N.,
RA   Holroyd S., Jagels K., Moule S., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G.,
RA   Parkhill J.;
RT   "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT   NCTC13129.";
RL   Nucleic Acids Res. 31:6516-6523(2003).
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; BX248356; CAE49568.1; -; Genomic_DNA.
DR   RefSeq; WP_010934767.1; NC_002935.2.
DR   AlphaFoldDB; Q6NHT3; -.
DR   SMR; Q6NHT3; -.
DR   STRING; 257309.DIP1048; -.
DR   KEGG; cdi:DIP1048; -.
DR   HOGENOM; CLU_079215_5_2_11; -.
DR   Proteomes; UP000002198; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045259; C:proton-transporting ATP synthase complex; IEA:InterPro.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:TreeGrafter.
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; NF004412; PRK05759.1-3; 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.
PE   3: Inferred from homology;
KW   ATP synthesis; Cell membrane; CF(0); Hydrogen ion transport; Ion transport;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..188
FT                   /note="ATP synthase subunit b"
FT                   /id="PRO_0000368436"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
SQ   SEQUENCE   188 AA;  21009 MW;  618A408CFCDFF849 CRC64;
     MTNVIKYLAE GEALPLEDHP SVLLPASYDI VWSLVVFIIV LILFWKFVRP KYQEVLTERE
     DRIKGGIQRA EAAQAEAKAA LEKYNAQLAE ARAEAAEIRE EARAKGKQIE AEMKAKATEE
     SNRIIESGEK QLAAQREQVV TELRREMGQN SISLAERLLG DQLSDDVKRS GTIDKFLAEL
     DTVSPAGK
//