ATPF2_RHOBA
ID ATPF2_RHOBA Reviewed; 242 AA.
AC Q7UFB9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 25-MAY-2022, entry version 91.
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}; OrderedLocusNames=RB10211;
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 -!- SEQUENCE CAUTION:
CC Sequence=CAD78764.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX294151; CAD78764.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_869307.1; NC_005027.1.
DR RefSeq; WP_007334260.1; NC_005027.1.
DR AlphaFoldDB; Q7UFB9; -.
DR SMR; Q7UFB9; -.
DR STRING; 243090.RB10211; -.
DR EnsemblBacteria; CAD78764; CAD78764; RB10211.
DR KEGG; rba:RB10211; -.
DR PATRIC; fig|243090.15.peg.4929; -.
DR eggNOG; COG0711; Bacteria.
DR HOGENOM; CLU_079215_2_0_0; -.
DR InParanoid; Q7UFB9; -.
DR OrthoDB; 1999641at2; -.
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; 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; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..242
FT /note="ATP synthase subunit b 2"
FT /id="PRO_0000368719"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
FT REGION 43..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 242 AA; 25894 MW; 5D129F2F740DF977 CRC64;
MKRLLAISSL TLLASLVLLV VSPARSLAAQ DEVTVVDALA DAADSEDGDH DHDHEGDDHG
HDEAAGDEHG HGDGDHAATP LLSFDGGSAI WNLIIFLCVL AILSKFVWPA VLGGLQAREE
KIREDLESAE KASAEAKQML SDYQLKLDEA ASQVQTMLAD ARRDAEANGQ KIVDAAKVEA
AAQRERALSD IENAKKVAMA EMAGQTSKLA MQVARSVVGR ELSADDHADL IRQSMERLPS
QN
