ID   ATPF_ILYTA              Reviewed;         163 AA.
AC   Q8KRV2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 67.
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;
OS   Ilyobacter tartaricus.
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Ilyobacter.
OX   NCBI_TaxID=167644;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-29.
RC   STRAIN=ATCC 35898 / DSM 2382;
RX   PubMed=12531483; DOI=10.1016/s0167-4781(02)00625-5;
RA   Meier T., von Ballmoos C., Neumann S., Kaim G.;
RT   "Complete DNA sequence of the atp operon of the sodium-dependent F1Fo ATP
RT   synthase from Ilyobacter tartaricus and identification of the encoded
RT   subunits.";
RL   Biochim. Biophys. Acta 1625:221-226(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 (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:0000250}; Single-pass
CC       membrane protein {ECO:0000250}.
CC   -!- MISCELLANEOUS: The ATPase of I.tartaricus is of special interest
CC       because it uses sodium ions instead of protons as the physiological
CC       coupling ion.
CC   -!- SIMILARITY: Belongs to the ATPase B chain family. {ECO:0000305}.
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DR   EMBL; AF522463; AAM94909.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8KRV2; -.
DR   SMR; Q8KRV2; -.
DR   PRIDE; Q8KRV2; -.
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..163
FT                   /note="ATP synthase subunit b, sodium ion specific"
FT                   /id="PRO_0000368530"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        17
FT                   /note="W -> I (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        21
FT                   /note="Missing (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   163 AA;  18718 MW;  467D28D0319AE574 CRC64;
     MAPQNMPAVS IDINMFWQII NFLILMFFFK KYFQKPISKV LDARKEKIAN ELKQAEIDRE
     MAAKANEETQ GILKAARTEA NEILLRAEKK ADDRKEAILK EANSQREKTI KSAELEVEKM
     KKQARKELQS EVTALAVNLA EKMINEKLDS KLGANLLNVL LKR