ID   ATPB_PROMO              Reviewed;         467 AA.
AC   P29707;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=ATP synthase subunit beta, sodium ion specific;
DE            EC=7.2.2.1;
DE   AltName: Full=Na(+)-translocating ATPase subunit beta;
GN   Name=atpD {ECO:0000255|HAMAP-Rule:MF_01347}; Synonyms=uncD;
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;
RA   Amann R., Ludwig W., Laubinger W., Dimroth P., Schleifer K.H.;
RT   "Cloning and sequencing of the gene encoding the beta subunit of the sodium
RT   ion translocating ATP synthase of Propionigenium modestum.";
RL   FEMS Microbiol. Lett. 56:253-260(1988).
RN   [2]
RP   SEQUENCE REVISION.
RX   PubMed=7556212; DOI=10.1111/j.1432-1033.1995.tb20849.x;
RA   Gerike U., Kaim G.W., Dimroth P.;
RT   "In vivo synthesis of ATPase complexes of Propionigenium modestum and
RT   Escherichia coli and analysis of their function.";
RL   Eur. J. Biochem. 232:596-602(1995).
RN   [3]
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: Produces ATP from ADP in the presence of a sodium ion
CC       gradient across the membrane. The beta chain is the catalytic subunit.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + 4 Na(+)(in) = ADP + H(+) + 4 Na(+)(out) +
CC         phosphate; Xref=Rhea:RHEA:58156, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.1;
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC       subunits: a, b and c.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01347};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01347}.
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 alpha/beta chains family.
CC       {ECO:0000255|HAMAP-Rule:MF_01347}.
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DR   EMBL; X58461; CAA41374.1; -; Genomic_DNA.
DR   PIR; S66664; S66664.
DR   AlphaFoldDB; P29707; -.
DR   SMR; P29707; -.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR   GO; GO:0046932; F:sodium-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR   GO; GO:0046962; F:sodium-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.1140.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01347; ATP_synth_beta_bact; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR005722; ATP_synth_F1_bsu.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR   InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR024034; ATPase_F1/V1_b/a_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF50615; SSF50615; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01039; atpD; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   1: Evidence at protein level;
KW   ATP synthesis; ATP-binding; Cell membrane; CF(1);
KW   Direct protein sequencing; Ion transport; Membrane; Nucleotide-binding;
KW   Sodium; Sodium transport; Translocase; Transport.
FT   CHAIN           1..467
FT                   /note="ATP synthase subunit beta, sodium ion specific"
FT                   /id="PRO_0000144461"
FT   BINDING         151..158
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   467 AA;  50850 MW;  8363DCF2896C25B3 CRC64;
     MENKGVITQI IGPVVDVTFE NELPRIYNAL KIDRGNGEYL VAEVQQHLGN SVVRAVAMDA
     TDGLQRGMEV VDTGPAITVP VGKAVLGRIL NVLGEPVDEA GEVKAEEYAP IHREAPAFED
     QGTEKEVFET GIKVVDLLAP YVKGGKIGLF GGAGVGKTVL IMELINNIAQ GHGGLSVFAG
     VGERTREGRD LYDEMLESGV LDKTSLVYGQ MNEPPGARLR VGLTGLTMAE NFRDKEGQDV
     LFFVDNIFRF TQAPSEVSAL LGRMPSAVGY QPNLATDMGA LQERITSTKT GSITSVQAVY
     VPADDLTDPA PATTFTHLDA TTVLSRRIAS LGIYPAVDPL DSTSTALEPQ IIGHEHYNTA
     REVQQILQRY KELQDIIAIL GMDELSDEDK VTVNRARKIE RFFSQPFHVA EQFTGMDGKY
     VTVKETIRGF KEIIEGKHDD LPEQAFLYVG TIDEAIAKAR ELMKGAE