ATPF2_SYNAS
ID ATPF2_SYNAS Reviewed; 274 AA.
AC Q2LY33;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 84.
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};
GN OrderedLocusNames=SYNAS_31170; ORFNames=SYN_02103;
OS Syntrophus aciditrophicus (strain SB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophales; Syntrophaceae;
OC Syntrophus.
OX NCBI_TaxID=56780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB;
RX PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA Campbell J.W., Gunsalus R.P.;
RT "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT of microbial growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
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; CP000252; ABC78996.1; -; Genomic_DNA.
DR RefSeq; WP_011419010.1; NC_007759.1.
DR AlphaFoldDB; Q2LY33; -.
DR SMR; Q2LY33; -.
DR STRING; 56780.SYN_02103; -.
DR EnsemblBacteria; ABC78996; ABC78996; SYN_02103.
DR KEGG; sat:SYN_02103; -.
DR eggNOG; COG0711; Bacteria.
DR HOGENOM; CLU_070737_0_0_7; -.
DR OMA; DWFTVIA; -.
DR OrthoDB; 1456190at2; -.
DR Proteomes; UP000001933; 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 Pfam; PF00430; ATP-synt_B; 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..274
FT /note="ATP synthase subunit b 2"
FT /id="PRO_0000368836"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
SQ SEQUENCE 274 AA; 31973 MW; 04B7ED4B972E05F3 CRC64;
MHIDWFVLLA QLVNFLILIY LLKRFLYTRI IQAMNEREAK IAARFDEAER LKREAEEAAR
VYEEKNSFLQ GQEEKMLNQA REVVNHRQKE WMDSAREEVD AIRRRWIETV LQEKAAFLEH
LRQRTGKQVF AIARKILDDL ADTAIESKMV DVLIDRIHSL DPAEREKICS ALEDSEEGAI
VQSAFALFPE DRQRLTDTVR DLLGKPDAVI RYQESSDLIG GIEFLASGHR IAWSISDYLE
HLEQDFDRVL HEEVRQTLPK PSGESVMPSE EQRP
