ATP6_BRUME
ID ATP6_BRUME Reviewed; 249 AA.
AC Q8YFH6; O68817;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=ATP synthase subunit a {ECO:0000255|HAMAP-Rule:MF_01393};
DE AltName: Full=ATP synthase F0 sector subunit a {ECO:0000255|HAMAP-Rule:MF_01393};
DE AltName: Full=F-ATPase subunit 6 {ECO:0000255|HAMAP-Rule:MF_01393};
GN Name=atpB {ECO:0000255|HAMAP-Rule:MF_01393}; OrderedLocusNames=BMEI1546;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 69-249.
RC STRAIN=133;
RX PubMed=11252353; DOI=10.1089/omi.1.2000.5.163;
RA Hernandez-Castro R., Verdugo-Rodriguez A., Gutierrez-Pabello J.A.,
RA Adams L.G., Suarez-Guemes F., Sahagun-Ruiz A.;
RT "Identification of four genes of the Brucella melitensis ATP synthase
RT operon F0 sector: relationship with the Rhodospirillaceae family.";
RL Microb. Comp. Genomics 5:163-171(2000).
CC -!- FUNCTION: Key component of the proton channel; it plays a direct role
CC in the translocation of protons across the membrane.
CC {ECO:0000255|HAMAP-Rule:MF_01393}.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an
CC alternating ring which encloses part of the gamma chain. CF(1) is
CC attached to CF(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_01393}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01393}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01393}.
CC -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000255|HAMAP-
CC Rule:MF_01393}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC08028.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAL52727.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE008917; AAL52727.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF054609; AAC08028.1; ALT_INIT; Genomic_DNA.
DR PIR; AD3445; AD3445.
DR RefSeq; WP_002963543.1; NZ_GG703778.1.
DR AlphaFoldDB; Q8YFH6; -.
DR SMR; Q8YFH6; -.
DR STRING; 224914.BMEI1546; -.
DR EnsemblBacteria; AAL52727; AAL52727; BMEI1546.
DR GeneID; 45051503; -.
DR GeneID; 55590149; -.
DR KEGG; bme:BMEI1546; -.
DR KEGG; bmel:DK63_1947; -.
DR PATRIC; fig|224914.52.peg.2048; -.
DR eggNOG; COG0356; Bacteria.
DR PhylomeDB; Q8YFH6; -.
DR Proteomes; UP000000419; Chromosome I.
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 Gene3D; 1.20.120.220; -; 1.
DR HAMAP; MF_01393; ATP_synth_a_bact; 1.
DR InterPro; IPR000568; ATP_synth_F0_asu.
DR InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR InterPro; IPR045083; ATP_synth_F0_asu_bact/mt.
DR InterPro; IPR035908; F0_ATP_A_sf.
DR PANTHER; PTHR11410; PTHR11410; 1.
DR Pfam; PF00119; ATP-synt_A; 1.
DR PRINTS; PR00123; ATPASEA.
DR SUPFAM; SSF81336; SSF81336; 1.
DR TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1.
DR PROSITE; PS00449; ATPASE_A; 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..249
FT /note="ATP synthase subunit a"
FT /id="PRO_0000362256"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT VARIANT 171
FT /note="S -> T (in strain: 133)"
FT VARIANT 189..191
FT /note="VFA -> FSP (in strain: 133)"
SQ SEQUENCE 249 AA; 26979 MW; 0322177F778BAE6D CRC64;
MANDPIHQFQ VSRWIPIDVG GVDLSFTNVS AFMVATVVLA SGFLYLTSSG RGLIPTRLQS
VSEMAYEFVA TSLRDSAGSK GMKFFPFVFS LFMFVLVANF IGLFPYFYTV TSQIIVTFAL
SLLVIGTVIF YGFFKHGFGF LKLFVPSGVP GIIVPLVVLI EIISFLSRPI SLSVRLFANM
LAGHITLKVF AGFVVSLSSL GALGIGGAVL PLLMTVAITA LEFLVAFLQA YVFTVLTCMY
INDAVHPGH
