ATPA_MYCPN
ID ATPA_MYCPN Reviewed; 518 AA.
AC Q50329; Q50344;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=ATP synthase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
DE EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01346};
DE AltName: Full=ATP synthase F1 sector subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
DE AltName: Full=F-ATPase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
GN Name=atpA {ECO:0000255|HAMAP-Rule:MF_01346}; OrderedLocusNames=MPN_600;
GN ORFNames=MP242;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-113.
RC STRAIN=ATCC 29342 / M129;
RX PubMed=7984111; DOI=10.1111/j.1365-2958.1994.tb00427.x;
RA Proft T., Herrmann R.;
RT "Identification and characterization of hitherto unknown Mycoplasma
RT pneumoniae proteins.";
RL Mol. Microbiol. 13:337-348(1994).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The alpha chain is a regulatory subunit.
CC {ECO:0000255|HAMAP-Rule:MF_01346}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01346};
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_01346}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01346};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01346}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01346}.
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DR EMBL; U43738; AAC43657.1; -; Genomic_DNA.
DR EMBL; U00089; AAB95890.1; -; Genomic_DNA.
DR EMBL; Z32649; CAA83571.1; -; Genomic_DNA.
DR PIR; S62847; S62847.
DR RefSeq; NP_110289.1; NC_000912.1.
DR RefSeq; WP_010874957.1; NC_000912.1.
DR AlphaFoldDB; Q50329; -.
DR SMR; Q50329; -.
DR IntAct; Q50329; 2.
DR STRING; 272634.MPN_600; -.
DR EnsemblBacteria; AAB95890; AAB95890; MPN_600.
DR KEGG; mpn:MPN_600; -.
DR PATRIC; fig|272634.6.peg.663; -.
DR HOGENOM; CLU_010091_2_1_14; -.
DR OMA; LQAPGVM; -.
DR BioCyc; MetaCyc:MON-538; -.
DR BioCyc; MPNE272634:G1GJ3-975-MON; -.
DR Proteomes; UP000000808; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR CDD; cd18113; ATP-synt_F1_alpha_C; 1.
DR CDD; cd01132; F1_ATPase_alpha; 1.
DR Gene3D; 1.20.150.20; -; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR000793; ATP_synth_asu_C.
DR InterPro; IPR038376; ATP_synth_asu_C_sf.
DR InterPro; IPR033732; ATP_synth_F1_a.
DR InterPro; IPR005294; ATP_synth_F1_asu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF00306; ATP-synt_ab_C; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00962; atpA; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW ATP synthesis; ATP-binding; Cell membrane; CF(1); Hydrogen ion transport;
KW Ion transport; Membrane; Nucleotide-binding; Reference proteome;
KW Translocase; Transport.
FT CHAIN 1..518
FT /note="ATP synthase subunit alpha"
FT /id="PRO_0000144337"
FT BINDING 169..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT SITE 362
FT /note="Required for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT CONFLICT 111..113
FT /note="LGE -> WEN (in Ref. 3; CAA83571)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 518 AA; 57375 MW; DA0ACBFA31C1C368 CRC64;
MADKLNEYVA LIKNEIKKYS KQIFNSEIGK VISVADGIAK VSGLENALLN ELIEFENNVQ
GIALNLEQNT VGVALFGDYS KIREGSTAKR THNVMQTPVG DVMLGRIVNA LGEPVDGRGP
IKAEEFDQVE KIAPGVMTRK TVNQPLETGI LTIDALFPIG KGQRELIVGD RQTGKTSIAI
DTIINQRGKD VYCVYVAMGQ KNSSVAQIVH QLEVTDSMKY TTVVCATASD PASMIYLTPF
TGITIAEYWL KQGKDVLIVF DDLSKHAIAY RTLSLLLRRP PGREAFPGDV FYLHSRLLER
ACRLNEEHGG GSITALPIIE TQAGDISAYI PTNVISITDG QLFMVSNLFN SGQRPAIHVG
LSVSRVGSAA QIKAIKQQTG SLKLELAQYS ELDSFSQFGS DLDENTKQIL ERGKRVMEMI
KQPNGKPYSQ THEALFLFAI AKSFIKFIPL DYIAKFKQRI MEEFDKEHPI YKEIATQKSF
SEALEAQTNT AFKALVKRFV SALPDYDITK YGTMEELE
