ATPB_MYCS2
ID ATPB_MYCS2 Reviewed; 475 AA.
AC A0R200; I7GEE5;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=ATP synthase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
DE EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01347};
DE AltName: Full=ATP synthase F1 sector subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
DE AltName: Full=F-ATPase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
GN Name=atpD {ECO:0000255|HAMAP-Rule:MF_01347};
GN OrderedLocusNames=MSMEG_4936, MSMEI_4809;
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 catalytic sites are hosted primarily by the
CC beta subunits. {ECO:0000255|HAMAP-Rule:MF_01347}.
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_01347};
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_01347}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01347};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01347}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01347}.
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DR EMBL; CP000480; ABK74032.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP41254.1; -; Genomic_DNA.
DR RefSeq; WP_003896328.1; NZ_SIJM01000067.1.
DR RefSeq; YP_889188.1; NC_008596.1.
DR PDB; 6FOC; X-ray; 4.00 A; D/E/F=1-475.
DR PDB; 7JG5; EM; 3.40 A; D/E/F=1-475.
DR PDB; 7JG6; EM; 3.70 A; D/E/F=1-475.
DR PDB; 7JG7; EM; 3.50 A; D/E/F=1-475.
DR PDB; 7JG8; EM; 3.30 A; D/E/F=1-475.
DR PDB; 7JG9; EM; 3.40 A; D/E/F=1-475.
DR PDB; 7JGA; EM; 3.20 A; D/E/F=1-475.
DR PDB; 7NJK; EM; 2.52 A; D/E/F=1-475.
DR PDB; 7NJL; EM; 2.71 A; D/E/F=1-475.
DR PDB; 7NJM; EM; 2.84 A; D/E/F=1-475.
DR PDB; 7NJN; EM; 2.64 A; D/E/F=1-475.
DR PDB; 7NJO; EM; 2.92 A; D/E/F=1-475.
DR PDB; 7NJP; EM; 2.84 A; D/E/F=1-475.
DR PDB; 7NJQ; EM; 2.67 A; D/E/F=1-475.
DR PDB; 7NJR; EM; 2.56 A; D/E/F=1-475.
DR PDB; 7NJS; EM; 2.46 A; D/E/F=1-475.
DR PDB; 7NK7; EM; 2.11 A; D/E/F=1-475.
DR PDB; 7NKD; EM; 3.12 A; D/E/F=1-475.
DR PDB; 7NKH; EM; 2.78 A; D/E/F=1-475.
DR PDB; 7NKJ; EM; 2.17 A; D/E/F=1-475.
DR PDB; 7NKL; EM; 3.67 A; D/E/F=1-475.
DR PDB; 7NKQ; EM; 2.98 A; D/E/F=1-475.
DR PDBsum; 6FOC; -.
DR PDBsum; 7JG5; -.
DR PDBsum; 7JG6; -.
DR PDBsum; 7JG7; -.
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; 7NKD; -.
DR PDBsum; 7NKH; -.
DR PDBsum; 7NKJ; -.
DR PDBsum; 7NKL; -.
DR PDBsum; 7NKQ; -.
DR AlphaFoldDB; A0R200; -.
DR SMR; A0R200; -.
DR STRING; 246196.MSMEI_4809; -.
DR PRIDE; A0R200; -.
DR EnsemblBacteria; ABK74032; ABK74032; MSMEG_4936.
DR EnsemblBacteria; AFP41254; AFP41254; MSMEI_4809.
DR GeneID; 66736258; -.
DR KEGG; msg:MSMEI_4809; -.
DR KEGG; msm:MSMEG_4936; -.
DR PATRIC; fig|246196.19.peg.4815; -.
DR eggNOG; COG0055; Bacteria.
DR OMA; GFNMIMD; -.
DR OrthoDB; 430176at2; -.
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 Gene3D; 1.10.1140.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01347; ATP_synth_beta_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005722; ATP_synth_F1_bsu.
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; IPR024034; ATPase_F1/V1_b/a_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01039; atpD; 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..475
FT /note="ATP synthase subunit beta"
FT /id="PRO_0000339549"
FT BINDING 160..167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
FT STRAND 10..16
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:7NJS"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:7JG5"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:7NJS"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 47..58
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:7NJS"
FT TURN 109..114
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 142..147
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:7NJS"
FT TURN 162..165
FT /evidence="ECO:0007829|PDB:7JG7"
FT HELIX 166..176
FT /evidence="ECO:0007829|PDB:7NJS"
FT TURN 177..180
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 182..191
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 194..206
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 224..243
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 257..267
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 283..293
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 302..309
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 318..324
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 335..339
FT /evidence="ECO:0007829|PDB:7NJS"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:7JG8"
FT HELIX 358..361
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 363..389
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 396..412
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 417..419
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 420..423
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 432..443
FT /evidence="ECO:0007829|PDB:7NJS"
FT TURN 444..449
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 452..455
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 461..470
FT /evidence="ECO:0007829|PDB:7NJS"
SQ SEQUENCE 475 AA; 51617 MW; 4BA3D2EA0A766397 CRC64;
MTATAEKTAG RVVRITGPVV DVEFPRGSVP ELFNALHAEI TFGALAKTLT LEVAQHLGDS
LVRCISMQPT DGLVRGVEVT DTGASISVPV GDGVKGHVFN ALGDCLDDPG YGKDFEHWSI
HRKPPAFSDL EPRTEMLETG LKVVDLLTPY VRGGKIALFG GAGVGKTVLI QEMINRIARN
FGGTSVFAGV GERTREGNDL WVELADANVL KDTALVFGQM DEPPGTRMRV ALSALTMAEF
FRDEQGQDVL LFIDNIFRFT QAGSEVSTLL GRMPSAVGYQ PTLADEMGEL QERITSTRGR
SITSMQAVYV PADDYTDPAP ATTFAHLDAT TELSRAVFSK GIFPAVDPLA SSSTILDPAI
VGDEHYRVAQ EVIRILQRYK DLQDIIAILG IDELSEEDKQ LVNRARRIER FLSQNMMAAE
QFTGQPGSTV PLKETIEAFD KLTKGEFDHL PEQAFFLIGG LDDLAKKAES LGAKL
