ID   ATPF2_METEP             Reviewed;         201 AA.
AC   A9VYW8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=ATP synthase subunit b 2;
DE   AltName: Full=ATP synthase F(0) sector subunit b 2;
DE   AltName: Full=ATPase subunit I 2;
DE   AltName: Full=F-type ATPase subunit b 2;
DE            Short=F-ATPase subunit b 2;
GN   Name=atpF2; Synonyms=atpG; OrderedLocusNames=Mext_3173;
OS   Methylorubrum extorquens (strain PA1) (Methylobacterium extorquens).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=419610;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Marx C., Richardson P.;
RT   "Complete sequence of Methylobacterium extorquens PA1.";
RL   Submitted (DEC-2007) 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 (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). The b'-subunit is a diverged
CC       and duplicated form of b found in plants and photosynthetic bacteria
CC       (By similarity). {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   -!- SIMILARITY: Belongs to the ATPase B chain family. {ECO:0000305}.
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DR   EMBL; CP000908; ABY31560.1; -; Genomic_DNA.
DR   RefSeq; WP_012254465.1; NC_010172.1.
DR   AlphaFoldDB; A9VYW8; -.
DR   SMR; A9VYW8; -.
DR   STRING; 419610.Mext_3173; -.
DR   EnsemblBacteria; ABY31560; ABY31560; Mext_3173.
DR   KEGG; mex:Mext_3173; -.
DR   eggNOG; COG0711; Bacteria.
DR   HOGENOM; CLU_079215_1_2_5; -.
DR   OMA; NQIFWLV; -.
DR   BioCyc; MEXT419610:MEXT_RS15950-MON; -.
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; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR   Pfam; PF00430; ATP-synt_B; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Cell inner membrane; Cell membrane; CF(0);
KW   Hydrogen ion transport; Ion transport; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..201
FT                   /note="ATP synthase subunit b 2"
FT                   /id="PRO_0000369011"
FT   TRANSMEM        47..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   201 AA;  21343 MW;  30281E4973AA3C47 CRC64;
     MAEQKNPLTT PSPNADTTIV PAGSPHTHTE QPSGGHGGAF PPFESHTFLS QLIWLALAFG
     LLYYLMSKVA LPRIEAILGN RAGRLSSDLT EAQRMKTEAD AAGAAYEKSL REAQAKAQAI
     AQETRNSLSA EADAKRKTLE AELNQRLAAS EATIRTRTTE AMGNVRAIAG ETASAIVERL
     TGQAPDQASL NRALDATPAV H