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ATPF2_RHIE6
ID   ATPF2_RHIE6             Reviewed;         207 AA.
AC   B3PRF8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=RHECIAT_CH0000956;
OS   Rhizobium etli (strain CIAT 652).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=491916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIAT 652;
RA   Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P.,
RA   Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J.,
RA   Palacios R., Davila G.;
RT   "Genome diversity and DNA divergence of Rhizobium etli.";
RL   Submitted (APR-2008) 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; CP001074; ACE89941.1; -; Genomic_DNA.
DR   RefSeq; WP_004675823.1; NC_010994.1.
DR   AlphaFoldDB; B3PRF8; -.
DR   SMR; B3PRF8; -.
DR   EnsemblBacteria; ACE89941; ACE89941; RHECIAT_CH0000956.
DR   GeneID; 45956293; -.
DR   KEGG; rec:RHECIAT_CH0000956; -.
DR   eggNOG; COG0711; Bacteria.
DR   HOGENOM; CLU_079215_1_2_5; -.
DR   OMA; NQIFWLV; -.
DR   Proteomes; UP000008817; 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   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..207
FT                   /note="ATP synthase subunit b 2"
FT                   /id="PRO_0000369032"
FT   TRANSMEM        53..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   207 AA;  21505 MW;  B901692A009604A5 CRC64;
     MFFVTPAYAE EAPAAATGTD AHAAPAAGEV HTETGVAEGE HARGPFPPFD STTYASQLLW
     LVITFSVFYL LMQKVIAPRI GAILDQRHTR ISQDLEEAGR LKAEADAAVQ TYEGELAAAR
     AKSNAIGSAA RDAAKAKAEE DRRAVEASLS EKIKAAEVRI ADIKAKAFAD VGTIAEETAA
     AVVEQLIGGT AAQADVAAAV AAAKKEA
 
 
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