ATPF_STRR6
ID ATPF_STRR6 Reviewed; 164 AA.
AC P0A2Z3; Q59952; Q59955;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 94.
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=spr1364;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
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 [3]
RP SUBUNIT, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=11580837; DOI=10.1046/j.1365-2958.2001.02597.x;
RA Martin-Galiano A.J., Ferrandiz M.J., de la Campa A.G.;
RT "The promoter of the operon encoding the F0F1 ATPase of Streptococcus
RT pneumoniae is inducible by pH.";
RL Mol. Microbiol. 41:1327-1338(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, ECO:0000269|PubMed:11580837}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:11580837};
CC Single-pass membrane protein {ECO:0000305|PubMed:11580837}.
CC -!- INDUCTION: Induced by a decrease in external pH from 7.5 to 5.7.
CC {ECO:0000269|PubMed:11580837}.
CC -!- SIMILARITY: Belongs to the ATPase B chain family. {ECO:0000255|HAMAP-
CC Rule:MF_01398}.
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DR EMBL; AE007317; AAL00168.1; -; Genomic_DNA.
DR EMBL; Z26851; CAA81454.1; -; Genomic_DNA.
DR PIR; C98042; C98042.
DR RefSeq; NP_358957.1; NC_003098.1.
DR RefSeq; WP_000558554.1; NC_003098.1.
DR AlphaFoldDB; P0A2Z3; -.
DR SMR; P0A2Z3; -.
DR STRING; 171101.spr1364; -.
DR EnsemblBacteria; AAL00168; AAL00168; spr1364.
DR GeneID; 60232701; -.
DR GeneID; 66806602; -.
DR KEGG; spr:spr1364; -.
DR PATRIC; fig|171101.6.peg.1478; -.
DR eggNOG; COG0711; Bacteria.
DR HOGENOM; CLU_079215_4_2_9; -.
DR OMA; FAWKPIL; -.
DR Proteomes; UP000000586; 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); IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP synthesis; Cell membrane; CF(0); Hydrogen ion transport; Ion transport;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..164
FT /note="ATP synthase subunit b"
FT /id="PRO_0000082390"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
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
