ID   ATPF2_NITMU             Reviewed;         291 AA.
AC   Q2Y8G8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=ATP synthase subunit b 2 {ECO:0000255|HAMAP-Rule:MF_01398};
DE   AltName: Full=ATP synthase F(0) sector subunit b 2 {ECO:0000255|HAMAP-Rule:MF_01398};
DE   AltName: Full=ATPase subunit I 2 {ECO:0000255|HAMAP-Rule:MF_01398};
DE   AltName: Full=F-type ATPase subunit b 2 {ECO:0000255|HAMAP-Rule:MF_01398};
DE            Short=F-ATPase subunit b 2 {ECO:0000255|HAMAP-Rule:MF_01398};
GN   Name=atpF2 {ECO:0000255|HAMAP-Rule:MF_01398}; OrderedLocusNames=Nmul_A1655;
OS   Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=323848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25196 / NCIMB 11849 / C 71;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC
RT   25196.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01398}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC       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; CP000103; ABB74953.1; -; Genomic_DNA.
DR   RefSeq; WP_011380976.1; NZ_FNVK01000021.1.
DR   AlphaFoldDB; Q2Y8G8; -.
DR   SMR; Q2Y8G8; -.
DR   STRING; 323848.Nmul_A1655; -.
DR   EnsemblBacteria; ABB74953; ABB74953; Nmul_A1655.
DR   KEGG; nmu:Nmul_A1655; -.
DR   eggNOG; COG0711; Bacteria.
DR   eggNOG; COG0712; Bacteria.
DR   HOGENOM; CLU_070737_0_0_4; -.
DR   OMA; DWFTVIA; -.
DR   OrthoDB; 1456190at2; -.
DR   Proteomes; UP000002718; 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; IPR017707; Alt_ATP_synth_F0_bsu.
DR   InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR   InterPro; IPR000711; ATPase_OSCP/dsu.
DR   Pfam; PF00430; ATP-synt_B; 1.
DR   Pfam; PF00213; OSCP; 1.
DR   TIGRFAMs; TIGR03321; alt_F1F0_F0_B; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Cell inner membrane; Cell membrane; CF(0);
KW   Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..291
FT                   /note="ATP synthase subunit b 2"
FT                   /id="PRO_0000368632"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
SQ   SEQUENCE   291 AA;  32355 MW;  40CFD1C07D61CDF9 CRC64;
     MLIDGFTVVA QIVNFLILVW LLKRFFYRPI LDALDERENR IASELAAATG KQREAEAELH
     RFRQKNEEFD QRREVLLTTV TDEVRAERQR LMEAAHADAD RIRISRNEAQ QREYQVLHDA
     IERRTCAEVL AITRKVLADL AGTTLEIHMT EAFIRRLRTL GPEEKAQLAV ALQAGGVESG
     HSATFQVFPP IVGQGSPSGI AVILVRSAFE LPAEQQEKIS TVIRETLKEE VRFNFGVEPN
     LISGIEMIAG GHKVAWSVAG YLASLEEEVS RLLNAKGAVG EGEAKSSTAA L