ID   ATPF2_ALBFT             Reviewed;         326 AA.
AC   Q21ZA0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Rfer_1167;
OS   Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS   (Rhodoferax ferrireducens).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=338969;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-621 / DSM 15236 / T118;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL   Submitted (FEB-2006) 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; CP000267; ABD68903.1; -; Genomic_DNA.
DR   RefSeq; WP_011463472.1; NC_007908.1.
DR   AlphaFoldDB; Q21ZA0; -.
DR   SMR; Q21ZA0; -.
DR   STRING; 338969.Rfer_1167; -.
DR   EnsemblBacteria; ABD68903; ABD68903; Rfer_1167.
DR   KEGG; rfr:Rfer_1167; -.
DR   eggNOG; COG0711; Bacteria.
DR   HOGENOM; CLU_070737_0_0_4; -.
DR   OMA; DWFTVIA; -.
DR   OrthoDB; 1456190at2; -.
DR   Proteomes; UP000008332; 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; IPR021327; DUF2934.
DR   Pfam; PF00430; ATP-synt_B; 1.
DR   Pfam; PF11154; DUF2934; 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..326
FT                   /note="ATP synthase subunit b 2"
FT                   /id="PRO_0000368717"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
FT   REGION          275..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..320
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   326 AA;  36758 MW;  A354849DF4967793 CRC64;
     MLIDWFTVVA QALNFLILVW LLKRFLYQPI LDAIDAREKR IALELADADT KRADAKRERD
     EFQQKNEVFD QQRAALLGKA MEEAKTERQR LLDDARHAAD ALATKRQEAL RSAQRSMSEA
     LSHRARDEVF AIARKALGDL ATTSLEERMG EVFTRRLREM DAKAKAALGE ALKTASEPAL
     VRSAFELPAD QRAAIQNAIN ETFSADIPLH FATAPEVVCG IELSTNGQKV GWSITDYLAS
     LEKGVDELLK ERDKAEPQSE LTRQIRKRAY ELYEQQGRKE GRAVQNWDKA ESEIRKENLS
     PAKTEPPPEA KAKPKPEEPK PEIGSP