ATPF1_RHOBA
ID ATPF1_RHOBA Reviewed; 246 AA.
AC Q7UH06;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=ATP synthase subunit b 1 {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=ATP synthase F(0) sector subunit b 1 {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=ATPase subunit I 1 {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=F-type ATPase subunit b 1 {ECO:0000255|HAMAP-Rule:MF_01398};
DE Short=F-ATPase subunit b 1 {ECO:0000255|HAMAP-Rule:MF_01398};
GN Name=atpF1 {ECO:0000255|HAMAP-Rule:MF_01398}; OrderedLocusNames=RB4915;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX294141; CAD78173.1; -; Genomic_DNA.
DR RefSeq; NP_866392.1; NC_005027.1.
DR RefSeq; WP_011120169.1; NC_005027.1.
DR AlphaFoldDB; Q7UH06; -.
DR SMR; Q7UH06; -.
DR STRING; 243090.RB4915; -.
DR EnsemblBacteria; CAD78173; CAD78173; RB4915.
DR KEGG; rba:RB4915; -.
DR PATRIC; fig|243090.15.peg.2339; -.
DR eggNOG; COG0711; Bacteria.
DR HOGENOM; CLU_070737_0_0_0; -.
DR InParanoid; Q7UH06; -.
DR OMA; DWFTVIA; -.
DR OrthoDB; 1456190at2; -.
DR Proteomes; UP000001025; 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); IBA:GO_Central.
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 InterPro; IPR000711; ATPase_OSCP/dsu.
DR Pfam; PF00430; ATP-synt_B; 1.
DR Pfam; PF00213; OSCP; 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..246
FT /note="ATP synthase subunit b 1"
FT /id="PRO_0000368718"
FT TRANSMEM 5..27
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
SQ SEQUENCE 246 AA; 28161 MW; C7C737CF5B7A5D73 CRC64;
MSIDWFTFTA QVINFLVLVG LLRYFLYAPI VRAMQAREQK VTQCLTDAET AKVEANQQRM
SLEKQTQLLQ ERREELLTKA KADADNERQR LIAEARKEAD TRREHWTSTF ERDQKDLADQ
TRRDIQRMGF QAARETVQQL ADEDLQKRVC QTFVKQLQTL GEDQLAAIAT QLADSGNPVL
VRSAKGLDSS DQNQIRDAIH RVFENKVEVR FESEPALIAG IEMDAGGYSL PWNAERTLKT
MEANVA
