ID H8KWX6_SOLCM Unreviewed; 164 AA.
AC H8KWX6;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=ATP synthase subunit b {ECO:0000256|HAMAP-Rule:MF_01398};
DE AltName: Full=ATP synthase F(0) sector subunit b {ECO:0000256|HAMAP-Rule:MF_01398};
DE AltName: Full=ATPase subunit I {ECO:0000256|HAMAP-Rule:MF_01398};
DE AltName: Full=F-type ATPase subunit b {ECO:0000256|HAMAP-Rule:MF_01398};
DE Short=F-ATPase subunit b {ECO:0000256|HAMAP-Rule:MF_01398};
GN Name=atpF {ECO:0000256|HAMAP-Rule:MF_01398};
GN OrderedLocusNames=Solca_3295 {ECO:0000313|EMBL:AFD08305.1};
OS Solitalea canadensis (strain ATCC 29591 / DSM 3403 / NBRC 15130 / NCIMB
OS 12057 / USAM 9D) (Flexibacter canadensis).
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Solitalea.
OX NCBI_TaxID=929556 {ECO:0000313|EMBL:AFD08305.1, ECO:0000313|Proteomes:UP000007590};
RN [1] {ECO:0000313|Proteomes:UP000007590}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29591 / DSM 3403 / NBRC 15130 / NCIMB 12057 / USAM 9D
RC {ECO:0000313|Proteomes:UP000007590};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Lu M.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Spring S., Schroeder M., Kopitz M., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Solitalea canadensis DSM 3403.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the F(0) channel, it forms part of the
CC peripheral stalk, linking F(1) to F(0). {ECO:0000256|HAMAP-
CC Rule:MF_01398}.
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.
CC {ECO:0000256|ARBA:ARBA00025198, ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_01398}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_01398}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01398}. Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the ATPase B chain family.
CC {ECO:0000256|ARBA:ARBA00005513, ECO:0000256|HAMAP-Rule:MF_01398,
CC ECO:0000256|RuleBase:RU003848}.
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; CP003349; AFD08305.1; -; Genomic_DNA.
DR RefSeq; WP_014681528.1; NC_017770.1.
DR AlphaFoldDB; H8KWX6; -.
DR STRING; 929556.Solca_3295; -.
DR KEGG; scn:Solca_3295; -.
DR eggNOG; COG0711; Bacteria.
DR HOGENOM; CLU_079215_4_1_10; -.
DR OrthoDB; 9795289at2; -.
DR Proteomes; UP000007590; Chromosome.
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 CDD; cd06503; ATP-synt_Fo_b; 1.
DR Gene3D; 1.20.5.620; F1F0 ATP synthase subunit B, membrane domain; 1.
DR HAMAP; MF_01398; ATP_synth_b_bprime; 1.
DR InterPro; IPR028987; ATP_synth_B-like_membr_sf.
DR InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR InterPro; IPR005864; ATP_synth_F0_bsu_bac.
DR NCBIfam; TIGR01144; ATP_synt_b; 1.
DR PANTHER; PTHR33445:SF1; ATP SYNTHASE SUBUNIT B; 1.
DR PANTHER; PTHR33445; ATP SYNTHASE SUBUNIT B', CHLOROPLASTIC; 1.
DR Pfam; PF00430; ATP-synt_B; 1.
DR SUPFAM; SSF81573; F1F0 ATP synthase subunit B, membrane domain; 1.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP-
KW Rule:MF_01398}; Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01398};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01398};
KW CF(0) {ECO:0000256|ARBA:ARBA00022547, ECO:0000256|HAMAP-Rule:MF_01398};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP-
KW Rule:MF_01398};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW Rule:MF_01398};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01398};
KW Reference proteome {ECO:0000313|Proteomes:UP000007590};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01398};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01398};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01398}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01398"
FT COILED 37..82
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 164 AA; 18305 MW; 4AAA63E1B80A7D23 CRC64;
MELVTPSIGL VFWTTITFIF LIILLGKFAW KPIVSALNER ERSIEDALSA ADKAKEELTR
LNQESDKLLK EARLERDKIL KEAKTMGDNL IADAKHNAQA EGAKMIAKAH EEINAQKNAA
LAEVKNQVAV LSIDIAEKVL RKKFENANDQ EALVAELLKD VKLN
//
