ATP6_MYCGA
ID ATP6_MYCGA Reviewed; 297 AA.
AC P33251;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 134.
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=MYCGA3000;
GN ORFNames=MGA_1164;
OS Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS (Mycoplasmoides gallisepticum).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=710127;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A5969Var.B;
RX PubMed=1386735; DOI=10.1042/bj2850881;
RA Rasmussen O.F., Shirvan M.H., Margalit H., Christiansen C., Rottem S.;
RT "Nucleotide sequence, organization and characterization of the atp genes
RT and the encoded subunits of Mycoplasma gallisepticum ATPase.";
RL Biochem. J. 285:881-888(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R(low / passage 15 / clone 2);
RX PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT "The complete genome sequence of the avian pathogen Mycoplasma
RT gallisepticum strain R(low).";
RL Microbiology 149:2307-2316(2003).
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 membrane {ECO:0000255|HAMAP-Rule:MF_01393};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01393}.
CC -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000255|HAMAP-
CC Rule:MF_01393}.
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DR EMBL; X64256; CAA45545.1; -; Genomic_DNA.
DR EMBL; AE015450; AAP56650.2; -; Genomic_DNA.
DR PIR; S24333; S24333.
DR RefSeq; WP_011113541.1; NC_004829.2.
DR AlphaFoldDB; P33251; -.
DR SMR; P33251; -.
DR KEGG; mga:MGA_1164; -.
DR PATRIC; fig|233150.7.peg.334; -.
DR HOGENOM; CLU_041018_3_0_14; -.
DR OMA; WNQPQLF; -.
DR OrthoDB; 867266at2; -.
DR Proteomes; UP000001418; 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 Gene3D; 1.20.120.220; -; 1.
DR HAMAP; MF_01393; ATP_synth_a_bact; 1.
DR InterPro; IPR045082; ATP_syn_F0_a_bact/chloroplast.
DR InterPro; IPR000568; ATP_synth_F0_asu.
DR InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR InterPro; IPR035908; F0_ATP_A_sf.
DR PANTHER; PTHR42823; PTHR42823; 1.
DR Pfam; PF00119; ATP-synt_A; 1.
DR PRINTS; PR00123; ATPASEA.
DR SUPFAM; SSF81336; SSF81336; 1.
DR PROSITE; PS00449; ATPASE_A; 1.
PE 3: Inferred from homology;
KW ATP synthesis; Cell membrane; CF(0); Hydrogen ion transport; Ion transport;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..297
FT /note="ATP synthase subunit a"
FT /id="PRO_0000082059"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT CONFLICT 223
FT /note="W -> G (in Ref. 1; CAA45545)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="A -> V (in Ref. 1; CAA45545)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="G -> R (in Ref. 1; CAA45545)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 297 AA; 33315 MW; DC4EC14A9547A40E CRC64;
MLPQEIVYTK LSSTETQNGW IDFLTTKPLA SQGIEWTPLI PTAHVLSIFM VLFMIAILTA
VYYTKLKKLK PTEPPTGYVL VVQLLILQFE NLTVDLLGEK NRRLSLLFII IFVYILISNL
MSMVGGIAAP TSSSTVTFSL GLMSFFGTFI MGVKYQKLAY FRDFFVIIKI KKKTIPLMIN
PLNVIGYFAP LLSISLRLWG NVLAGSIFIA LLYSLFRTFF TLWSPSSFSV GLVFGTLAGG
LVIPAFHVYF DILVSAIQAF VFVSLMLTYW SQPIKAAENA AEEKGQQMIE NQRLNVK
