ID   ATPF2_METCA             Reviewed;         253 AA.
AC   Q603U6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=MCA2701;
OS   Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylococcus.
OX   NCBI_TaxID=243233;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX   PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA   Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA   Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA   Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J.,
RA   Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L.,
RA   Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H.,
RA   Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R.,
RA   Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.;
RT   "Genomic insights into methanotrophy: the complete genome sequence of
RT   Methylococcus capsulatus (Bath).";
RL   PLoS Biol. 2:1616-1628(2004).
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; AE017282; AAU91246.1; -; Genomic_DNA.
DR   RefSeq; WP_010961912.1; NC_002977.6.
DR   AlphaFoldDB; Q603U6; -.
DR   SMR; Q603U6; -.
DR   STRING; 243233.MCA2701; -.
DR   EnsemblBacteria; AAU91246; AAU91246; MCA2701.
DR   KEGG; mca:MCA2701; -.
DR   eggNOG; COG0711; Bacteria.
DR   eggNOG; COG0712; Bacteria.
DR   HOGENOM; CLU_070737_0_0_6; -.
DR   OMA; DWFTVIA; -.
DR   OrthoDB; 1456190at2; -.
DR   Proteomes; UP000006821; 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; 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.
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..253
FT                   /note="ATP synthase subunit b 2"
FT                   /id="PRO_0000368590"
FT   TRANSMEM        9..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
SQ   SEQUENCE   253 AA;  29045 MW;  B543E4E8A12650CD CRC64;
     MDLNPSTFVL EIVNFLVLVW LLKRFLYQPV SAAIEERRRQ IARTVAEARD TQTAAETLRM
     QYESRLADWE SEKRQAREAF KQEIEAERQR ALDELEKALD AEREKARVLI ERQRRDMESD
     LERQALRLSR QFASRFLERL AGPEMEAALL RMFGEDLAAM SPEQWQALTR ALEEQEHPEA
     EIASAFPLKP ESCAELTEMI EARTGRAVAW RFREDPALIC GIRLRAGHRV LAANVGEELK
     FFADGAENSL GGG