ATPA_MYCS2
ID ATPA_MYCS2 Reviewed; 548 AA.
AC A0R202; I7GD71;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 112.
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};
GN OrderedLocusNames=MSMEG_4938, MSMEI_4811;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS], AND CLEAVAGE OF INITIATOR METHIONINE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
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; CP000480; ABK72810.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP41256.1; -; Genomic_DNA.
DR RefSeq; WP_003896330.1; NZ_SIJM01000067.1.
DR RefSeq; YP_889190.1; NC_008596.1.
DR PDB; 6FOC; X-ray; 4.00 A; A/B/C=1-548.
DR PDB; 7JG8; EM; 3.30 A; A/B/C=1-548.
DR PDB; 7JG9; EM; 3.40 A; A/B/C=1-548.
DR PDB; 7JGA; EM; 3.20 A; A/B/C=1-548.
DR PDB; 7NJK; EM; 2.52 A; A/B/C=1-548.
DR PDB; 7NJL; EM; 2.71 A; A/B/C=1-548.
DR PDB; 7NJM; EM; 2.84 A; A/B/C=1-548.
DR PDB; 7NJN; EM; 2.64 A; A/B/C=1-548.
DR PDB; 7NJO; EM; 2.92 A; A/B/C=1-548.
DR PDB; 7NJP; EM; 2.84 A; A/B/C=1-548.
DR PDB; 7NJQ; EM; 2.67 A; A/B/C=1-548.
DR PDB; 7NJR; EM; 2.56 A; A/B/C=1-548.
DR PDB; 7NJS; EM; 2.46 A; A/B/C=1-548.
DR PDB; 7NK7; EM; 2.11 A; A/B/C=1-548.
DR PDB; 7NKB; EM; 2.90 A; C=1-548.
DR PDB; 7NKD; EM; 3.12 A; A/B/C=1-548.
DR PDB; 7NKH; EM; 2.78 A; A/B/C=1-548.
DR PDB; 7NKJ; EM; 2.17 A; A/B/C=1-548.
DR PDB; 7NKK; EM; 3.60 A; C=1-548.
DR PDB; 7NKL; EM; 3.67 A; A/B/C=1-548.
DR PDB; 7NKN; EM; 2.71 A; C=1-548.
DR PDB; 7NKQ; EM; 2.98 A; A/B/C=1-548.
DR PDB; 7NL9; EM; 2.86 A; C=1-548.
DR PDBsum; 6FOC; -.
DR PDBsum; 7JG8; -.
DR PDBsum; 7JG9; -.
DR PDBsum; 7JGA; -.
DR PDBsum; 7NJK; -.
DR PDBsum; 7NJL; -.
DR PDBsum; 7NJM; -.
DR PDBsum; 7NJN; -.
DR PDBsum; 7NJO; -.
DR PDBsum; 7NJP; -.
DR PDBsum; 7NJQ; -.
DR PDBsum; 7NJR; -.
DR PDBsum; 7NJS; -.
DR PDBsum; 7NK7; -.
DR PDBsum; 7NKB; -.
DR PDBsum; 7NKD; -.
DR PDBsum; 7NKH; -.
DR PDBsum; 7NKJ; -.
DR PDBsum; 7NKK; -.
DR PDBsum; 7NKL; -.
DR PDBsum; 7NKN; -.
DR PDBsum; 7NKQ; -.
DR PDBsum; 7NL9; -.
DR AlphaFoldDB; A0R202; -.
DR SMR; A0R202; -.
DR STRING; 246196.MSMEI_4811; -.
DR PRIDE; A0R202; -.
DR EnsemblBacteria; ABK72810; ABK72810; MSMEG_4938.
DR EnsemblBacteria; AFP41256; AFP41256; MSMEI_4811.
DR GeneID; 66736260; -.
DR KEGG; msg:MSMEI_4811; -.
DR KEGG; msm:MSMEG_4938; -.
DR PATRIC; fig|246196.19.peg.4817; -.
DR eggNOG; COG0056; Bacteria.
DR OMA; LQAPGVM; -.
DR OrthoDB; 837522at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00962; atpA; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; ATP-binding; Cell membrane; CF(1);
KW Hydrogen ion transport; Ion transport; Membrane; Nucleotide-binding;
KW Reference proteome; Translocase; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:18955433"
FT CHAIN 2..548
FT /note="ATP synthase subunit alpha"
FT /id="PRO_0000302669"
FT BINDING 172..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT SITE 373
FT /note="Required for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT HELIX 8..20
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 29..38
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:7NJS"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 90..103
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:7JG8"
FT HELIX 154..159
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:7JG8"
FT HELIX 178..188
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 190..195
FT /evidence="ECO:0007829|PDB:7NJS"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 202..210
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 213..225
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 231..237
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 243..261
FT /evidence="ECO:0007829|PDB:7NJS"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 266..272
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 274..287
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 301..309
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 323..331
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:7JG8"
FT HELIX 340..348
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 349..355
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 357..361
FT /evidence="ECO:0007829|PDB:7NJS"
FT TURN 370..372
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 374..377
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 378..381
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 384..389
FT /evidence="ECO:0007829|PDB:7NJS"
FT TURN 390..392
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 393..403
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:7NJS"
FT TURN 408..412
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 415..431
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 441..452
FT /evidence="ECO:0007829|PDB:7NJS"
FT TURN 453..458
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 461..463
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 464..478
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 480..489
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 494..510
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 514..516
FT /evidence="ECO:0007829|PDB:7NJN"
FT TURN 530..532
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 533..542
FT /evidence="ECO:0007829|PDB:7NJS"
SQ SEQUENCE 548 AA; 58889 MW; FE2623477FECEC16 CRC64;
MAELTISAAD IEGAIEDYVS SFSADTEREE IGTVIDAGDG IAHVEGLPSV MTQELLEFPG
GVLGVALNLD EHSVGAVILG EFEKIEEGQQ VKRTGEVLSV PVGDAFLGRV VNPLGQPIDG
QGDIAAETRR ALELQAPSVV QRQSVSEPLQ TGIKAIDAMT PIGRGQRQLI IGDRKTGKTA
VCVDTILNQR EAWLTGDPKQ QVRCVYVAIG QKGTTIASVK RALEEGGAME YTTIVAAPAS
DAAGFKWLAP YTGSAIGQHW MYNGKHVLIV FDDLSKQADA YRAISLLLRR PPGREAFPGD
VFYLHSRLLE RCAKLSDELG GGSMTGLPII ETKANDISAF IPTNVISITD GQCFLESDLF
NQGVRPAINV GVSVSRVGGA AQIKAMKEVA GSLRLDLSQY RELEAFAAFA SDLDAASKAQ
LDRGARLVEL LKQPQYSPLA VEEQVVAIFL GTQGHLDSVP VEDVQRFESE LLEHVKASHS
DIFDGIRETK KLSEEAEEKL VSVINEFKKG FQASDGSSVV VSENAEALDP EDLEKESVKV
RKPAPKKA
