ATPF2_AGRFC
ID ATPF2_AGRFC Reviewed; 213 AA.
AC Q7D0U9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 91.
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=Atu0716; ORFNames=AGR_C_1299;
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
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; AE007869; AAK86526.2; -; Genomic_DNA.
DR RefSeq; NP_353741.2; NC_003062.2.
DR RefSeq; WP_010971091.1; NC_003062.2.
DR AlphaFoldDB; Q7D0U9; -.
DR SMR; Q7D0U9; -.
DR STRING; 176299.Atu0716; -.
DR EnsemblBacteria; AAK86526; AAK86526; Atu0716.
DR KEGG; atu:Atu0716; -.
DR PATRIC; fig|176299.10.peg.714; -.
DR eggNOG; COG0711; Bacteria.
DR HOGENOM; CLU_079215_1_2_5; -.
DR OMA; NQIFWLV; -.
DR BioCyc; AGRO:ATU0716-MON; -.
DR Proteomes; UP000000813; Chromosome circular.
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; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..213
FT /note="ATP synthase subunit b 2"
FT /id="PRO_0000368997"
FT TRANSMEM 57..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 213 AA; 22033 MW; C1520E6DEEE25155 CRC64;
MFVTEAYAQS APTVGETHTE TPAVGQPQPE ATHTETGVAH GAEHGASGVF PPFDQSTYAS
QVLWLAITFG LFYLLMQKVI VPRVGGILEN RHGRIAQDLD EAARLKAEAD TAVETYEKEL
AAARAKASSI GASARDAAKA KADADRAAIE AGLAEKLAAA EKRIAGIRDH AFADVGAIAE
ETATAIVDQL VGAKVKDTDV KAAIAAASAV KGA
