ATPF_STRPN
ID ATPF_STRPN Reviewed; 164 AA.
AC P0A2Z2; Q59952; Q59955;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
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}; Synonyms=atpB;
GN OrderedLocusNames=SP_1512;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M222;
RX PubMed=7934882; DOI=10.1111/j.1365-2958.1994.tb01045.x;
RA Fenoll A., Munoz R., Garcia E., de la Campa A.G.;
RT "Molecular basis of the optochin-sensitive phenotype of pneumococcus:
RT characterization of the genes encoding the F0 complex of the Streptococcus
RT pneumoniae and Streptococcus oralis H(+)-ATPases.";
RL Mol. Microbiol. 12:587-598(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
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; Z26850; CAA81449.1; -; Genomic_DNA.
DR EMBL; AE005672; AAK75603.1; -; Genomic_DNA.
DR PIR; B95176; B95176.
DR PIR; S49401; S49401.
DR RefSeq; WP_000558554.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; P0A2Z2; -.
DR SMR; P0A2Z2; -.
DR STRING; 170187.SP_1512; -.
DR EnsemblBacteria; AAK75603; AAK75603; SP_1512.
DR GeneID; 60232701; -.
DR GeneID; 66806602; -.
DR KEGG; spn:SP_1512; -.
DR eggNOG; COG0711; Bacteria.
DR OMA; FAWKPIL; -.
DR PhylomeDB; P0A2Z2; -.
DR BioCyc; SPNE170187:G1FZB-1528-MON; -.
DR Proteomes; UP000000585; 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; 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 Pfam; PF00430; ATP-synt_B; 1.
DR SUPFAM; SSF81573; SSF81573; 1.
DR TIGRFAMs; TIGR01144; ATP_synt_b; 1.
PE 3: Inferred from homology;
KW ATP synthesis; Cell membrane; CF(0); Hydrogen ion transport; Ion transport;
KW Membrane; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..164
FT /note="ATP synthase subunit b"
FT /id="PRO_0000082389"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
FT CONFLICT 101
FT /note="L -> V (in Ref. 1; CAA81449)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="H -> R (in Ref. 1; CAA81449)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="V -> A (in Ref. 1; CAA81449)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="I -> V (in Ref. 1; CAA81449)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="Q -> K (in Ref. 1; CAA81449)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="A -> E (in Ref. 1; CAA81449)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 164 AA; 17987 MW; C72D9F2B638C5C62 CRC64;
MHVTVGELIG NFILITGSFI LLLVLIKKFA WSNITGIFEE RAEKIASDID RAEEARQKAE
VLAQKREDEL AGSRKEAKTI IENAKETAEQ SKANILADAK LEAGHLKEKA NQEIAQNKVE
ALQSVKGEVA DLTISLAGKI ISQNLDSHAH KALIDQYIDQ LGEA
