ATP6_MYCPN
ID ATP6_MYCPN Reviewed; 293 AA.
AC Q50326;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 123.
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=MPN_604;
GN ORFNames=MP238;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8604303; DOI=10.1093/nar/24.4.628;
RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.;
RT "Sequence analysis of 56 kb from the genome of the bacterium Mycoplasma
RT pneumoniae comprising the dnaA region, the atp operon and a cluster of
RT ribosomal protein genes.";
RL Nucleic Acids Res. 24:628-639(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
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; U43738; AAC43653.1; -; Genomic_DNA.
DR EMBL; U00089; AAB95886.1; -; Genomic_DNA.
DR PIR; S62843; S62843.
DR RefSeq; NP_110293.1; NC_000912.1.
DR RefSeq; WP_010874961.1; NC_000912.1.
DR AlphaFoldDB; Q50326; -.
DR SMR; Q50326; -.
DR STRING; 272634.MPN_604; -.
DR EnsemblBacteria; AAB95886; AAB95886; MPN_604.
DR GeneID; 66608711; -.
DR KEGG; mpn:MPN_604; -.
DR PATRIC; fig|272634.6.peg.667; -.
DR HOGENOM; CLU_041018_3_0_14; -.
DR OMA; WNQPQLF; -.
DR BioCyc; MetaCyc:MON-535; -.
DR BioCyc; MPNE272634:G1GJ3-979-MON; -.
DR Proteomes; UP000000808; 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..293
FT /note="ATP synthase subunit a"
FT /id="PRO_0000082062"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
SQ SEQUENCE 293 AA; 33004 MW; AFC833C49331E2EA CRC64;
MSPRAIVLKE PNGVNLVPHE GIFDISPVAG WKPLLPTDQV FGIFVVFIVL LTLFLVYWIK
LRKADPLRNH SSFVLLMQML FVWAQDTTAD LIGEENKKFT PYFLMLLLYL VSSNLIGLLG
GISPPTSSLT FTFSLGLATF LGIVIMGIRY QRWSFFKSFT FNITIKGKKY STLIPNPLSF
LGEFAPLFSI SLRLWGNILG GTLILALFYN FWFFAFSTLS NKPLALSLGA IFAGILTPAL
HVYFDVVVGT LQGYVFVMLT YNYWAKMRNI GLEESQEAAQ RLQNLEVAKE IIN
