ATPF_ANASK
ID ATPF_ANASK Reviewed; 179 AA.
AC B4UJU5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=ATP synthase subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=ATP synthase F(0) sector subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=ATPase subunit I {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=F-type ATPase subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
DE Short=F-ATPase subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
GN Name=atpF {ECO:0000255|HAMAP-Rule:MF_01398}; OrderedLocusNames=AnaeK_4474;
OS Anaeromyxobacter sp. (strain K).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter;
OC unclassified Anaeromyxobacter.
OX NCBI_TaxID=447217;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikiva G.,
RA Beliaev A.;
RT "Complete sequence of Anaeromyxobacter sp. K.";
RL Submitted (AUG-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. {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; CP001131; ACG75676.1; -; Genomic_DNA.
DR RefSeq; WP_012528420.1; NC_011145.1.
DR AlphaFoldDB; B4UJU5; -.
DR SMR; B4UJU5; -.
DR EnsemblBacteria; ACG75676; ACG75676; AnaeK_4474.
DR KEGG; ank:AnaeK_4474; -.
DR HOGENOM; CLU_079215_4_1_7; -.
DR OMA; FAWKPIL; -.
DR OrthoDB; 1999641at2; -.
DR Proteomes; UP000001871; 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; IPR005864; ATP_synth_F0_bsu_bac.
DR Pfam; PF00430; ATP-synt_B; 1.
DR TIGRFAMs; TIGR01144; 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..179
FT /note="ATP synthase subunit b"
FT /id="PRO_0000368312"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
SQ SEQUENCE 179 AA; 19593 MW; 71DE4364728E38E0 CRC64;
MASFLSPVPV LAAGGIADIN PGLTLWTAIT FLVMLVVLGK FAWGPIVKML AERERSIREA
IDSAKKERAE AERLLAAQKE SLAKAQREAA ELARRNQQEV EALRQELTAK ARKEADELVA
EARRQIAEEL GKAKTELKAQ VVDLAIDAAS RLVKANLDEK AQRALVEEYI AQLPANRAA