ATPF_PROMO
ID ATPF_PROMO Reviewed; 168 AA.
AC P21904;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 2.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=ATP synthase subunit b, sodium ion specific;
DE AltName: Full=ATP synthase F(0) sector subunit b;
DE AltName: Full=ATPase subunit I;
DE AltName: Full=F-type ATPase subunit b;
DE Short=F-ATPase subunit b;
GN Name=atpF; Synonyms=uncF;
OS Propionigenium modestum.
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Propionigenium.
OX NCBI_TaxID=2333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 2376 / Gra Succ2;
RX PubMed=2174545; DOI=10.1093/nar/18.22.6697;
RA Kaim G.W., Ludwig W., Dimroth P., Schleifer K.H.;
RT "Sequence of subunits a and b of the sodium ion translocating adenosine
RT triphosphate synthase of Propionigenium modestum.";
RL Nucleic Acids Res. 18:6697-6697(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 2376 / Gra Succ2;
RX PubMed=1386022; DOI=10.1111/j.1432-1033.1992.tb17072.x;
RA Kaim G.W., Ludwig W., Dimroth P., Schleifer K.H.;
RT "Cloning, sequencing and in vivo expression of genes encoding the F0 part
RT of the sodium-ion-dependent ATP synthase of Propionigenium modestum in
RT Escherichia coli.";
RL Eur. J. Biochem. 207:463-470(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 2376 / Gra Succ2;
RX PubMed=2170948; DOI=10.1093/nar/18.19.5887;
RA Esser U., Krumholz L.R., Simoni R.D.;
RT "Nucleotide sequence of the F0 subunits of the sodium dependent F1F0 ATPase
RT of Propionigenium modestum.";
RL Nucleic Acids Res. 18:5887-5888(1990).
RN [4]
RP PROTEIN SEQUENCE OF 1-7.
RX PubMed=8422943; DOI=10.1016/0014-5793(93)81742-i;
RA Gerike U., Dimroth P.;
RT "N-terminal amino acid sequences of the subunits of the Na(+)-translocating
RT F1F0 ATPase from Propionigenium modestum.";
RL FEBS Lett. 316:89-92(1993).
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 (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: Component of the F(0) channel, it forms part of the
CC peripheral stalk, linking F(1) to F(0). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- MISCELLANEOUS: The ATPase of P.modestum is of special interest because
CC it uses sodium ions instead of protons as the physiological coupling
CC ion.
CC -!- SIMILARITY: Belongs to the ATPase B chain family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA38580.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA41370.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA46896.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X54810; CAA38580.1; ALT_INIT; Genomic_DNA.
DR EMBL; X66102; CAA46896.1; ALT_INIT; Genomic_DNA.
DR EMBL; X53960; CAA37913.1; -; Genomic_DNA.
DR EMBL; X58461; CAA41370.1; ALT_INIT; Genomic_DNA.
DR PIR; S23323; S23323.
DR AlphaFoldDB; P21904; -.
DR SMR; P21904; -.
DR TCDB; 3.A.2.1.2; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
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 GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
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 inner membrane; Cell membrane; CF(0);
KW Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane;
KW Sodium; Sodium transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..168
FT /note="ATP synthase subunit b, sodium ion specific"
FT /id="PRO_0000082383"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 168 AA; 19201 MW; 461EA7572AF8ABDA CRC64;
MAPQNMPAVS IDINMFWQII NFLILMFFFK KYFQKPIAKV LDARKEKIAN DLKQAEIDKE
MAAKANGEAQ GIVKSAKTEA NEMLLRAEKK ADERKETILK EANTQREKML KSAEVEIEKM
KEQARKELQL EVTDLAVKLA EKMINEKVDA KIGANLLDQF IGEVGEEK
