ATPFD_MYCS2
ID ATPFD_MYCS2 Reviewed; 445 AA.
AC A0R203; I7G6D5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=ATP synthase subunit b-delta;
DE Includes:
DE RecName: Full=ATP synthase subunit b;
DE AltName: Full=ATP synthase F(0) sector subunit b 2;
DE AltName: Full=ATPase subunit I 2;
DE AltName: Full=F-type ATPase subunit b 2;
DE Short=F-ATPase subunit b 2;
DE Includes:
DE RecName: Full=ATP synthase subunit delta;
DE AltName: Full=ATP synthase F(1) sector subunit delta;
DE AltName: Full=F-type ATPase subunit delta;
DE Short=F-ATPase subunit delta;
GN Name=atpFH; Synonyms=atpF, atpH; OrderedLocusNames=MSMEG_4939, MSMEI_4812;
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], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
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: F(1)F(0) ATP synthase produces ATP from ADP in the presence
CC of a proton or sodium gradient. F-type ATPases consist of two
CC structural domains, F(1) containing the extramembraneous catalytic core
CC and F(0) containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: This fusion protein includes a component of the F(0) channel
CC (subunit b) and of the F(1) subunit (subunit delta). Two copies of
CC subunit b and one of delta together form the peripheral 'stator' stalk
CC which links F(1) to F(0) (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core
CC - and F(0) - the membrane proton channel. F(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main
CC subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an
CC alternating ring which encloses part of the gamma chain. F(1) is
CC attached to F(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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the ATPase B chain
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the ATPase delta
CC chain family. {ECO:0000305}.
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DR EMBL; CP000480; ABK71377.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP41257.1; -; Genomic_DNA.
DR RefSeq; WP_003896331.1; NZ_SIJM01000067.1.
DR RefSeq; YP_889191.1; NC_008596.1.
DR PDB; 7JG5; EM; 3.40 A; d=1-445.
DR PDB; 7JG6; EM; 3.70 A; d=1-445.
DR PDB; 7JG7; EM; 3.50 A; d=1-445.
DR PDB; 7JG8; EM; 3.30 A; d=1-445.
DR PDB; 7JG9; EM; 3.40 A; d=1-445.
DR PDB; 7JGA; EM; 3.20 A; d=1-445.
DR PDB; 7JGB; EM; 3.50 A; d=1-445.
DR PDB; 7JGC; EM; 3.40 A; d=1-445.
DR PDB; 7NJK; EM; 2.52 A; d=1-445.
DR PDB; 7NJL; EM; 2.71 A; d=1-445.
DR PDB; 7NJM; EM; 2.84 A; d=1-445.
DR PDB; 7NJN; EM; 2.64 A; d=1-445.
DR PDB; 7NJO; EM; 2.92 A; d=1-445.
DR PDB; 7NJP; EM; 2.84 A; d=1-445.
DR PDB; 7NJQ; EM; 2.67 A; d=1-445.
DR PDB; 7NJR; EM; 2.56 A; d=1-445.
DR PDB; 7NJS; EM; 2.46 A; d=1-445.
DR PDB; 7NJT; EM; 2.75 A; d=1-445.
DR PDB; 7NJU; EM; 3.74 A; d=1-445.
DR PDB; 7NJV; EM; 2.90 A; d=1-445.
DR PDB; 7NJW; EM; 3.67 A; d=1-445.
DR PDB; 7NJX; EM; 4.32 A; d=1-445.
DR PDB; 7NJY; EM; 2.94 A; d=1-445.
DR PDB; 7NK9; EM; 2.90 A; d=1-445.
DR PDB; 7NKD; EM; 3.12 A; d=1-445.
DR PDB; 7NKL; EM; 3.67 A; d=1-445.
DR PDB; 7NKP; EM; 4.06 A; d=1-445.
DR PDB; 7NKQ; EM; 2.98 A; d=1-445.
DR PDB; 7NL9; EM; 2.86 A; d=1-445.
DR PDBsum; 7JG5; -.
DR PDBsum; 7JG6; -.
DR PDBsum; 7JG7; -.
DR PDBsum; 7JG8; -.
DR PDBsum; 7JG9; -.
DR PDBsum; 7JGA; -.
DR PDBsum; 7JGB; -.
DR PDBsum; 7JGC; -.
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; 7NJT; -.
DR PDBsum; 7NJU; -.
DR PDBsum; 7NJV; -.
DR PDBsum; 7NJW; -.
DR PDBsum; 7NJX; -.
DR PDBsum; 7NJY; -.
DR PDBsum; 7NK9; -.
DR PDBsum; 7NKD; -.
DR PDBsum; 7NKL; -.
DR PDBsum; 7NKP; -.
DR PDBsum; 7NKQ; -.
DR PDBsum; 7NL9; -.
DR AlphaFoldDB; A0R203; -.
DR SMR; A0R203; -.
DR STRING; 246196.MSMEI_4812; -.
DR PRIDE; A0R203; -.
DR EnsemblBacteria; ABK71377; ABK71377; MSMEG_4939.
DR EnsemblBacteria; AFP41257; AFP41257; MSMEI_4812.
DR GeneID; 66736261; -.
DR KEGG; msg:MSMEI_4812; -.
DR KEGG; msm:MSMEG_4939; -.
DR PATRIC; fig|246196.19.peg.4818; -.
DR eggNOG; COG0711; Bacteria.
DR eggNOG; COG0712; Bacteria.
DR OMA; YVVPPVR; -.
DR OrthoDB; 1937493at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 HAMAP; MF_01398; ATP_synth_b_bprime; 1.
DR HAMAP; MF_01416; ATP_synth_delta_bact; 1.
DR InterPro; IPR028987; ATP_synth_B-like_membr_sf.
DR InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR InterPro; IPR000711; ATPase_OSCP/dsu.
DR PANTHER; PTHR11910; PTHR11910; 1.
DR Pfam; PF00430; ATP-synt_B; 1.
DR Pfam; PF00213; OSCP; 1.
DR SUPFAM; SSF81573; SSF81573; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; Cell membrane; CF(0); Hydrogen ion transport;
KW Ion transport; Membrane; Multifunctional enzyme; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..445
FT /note="ATP synthase subunit b-delta"
FT /id="PRO_0000368892"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..168
FT /note="ATP synthase subunit b"
FT REGION 169..445
FT /note="ATP synthase subunit delta"
FT HELIX 2..21
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 23..136
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 140..156
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 174..190
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:7NJR"
FT HELIX 196..215
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 217..224
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:7JG7"
FT HELIX 231..241
FT /evidence="ECO:0007829|PDB:7NJS"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 247..258
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 264..286
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 289..304
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 307..314
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 320..330
FT /evidence="ECO:0007829|PDB:7NJS"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 339..350
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 357..371
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 375..383
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 387..401
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 405..411
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 413..415
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 417..423
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 426..429
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 432..442
FT /evidence="ECO:0007829|PDB:7NJS"
SQ SEQUENCE 445 AA; 47450 MW; DD3CD70D05AD03EF CRC64;
MSIFIGQLIG FAVIAFIIVK WVVPPVRTLM RNQQEAVRAA LAESAEAAKK LADADAMHAK
ALADAKAESE KVTEEAKQDS ERIAAQLSEQ AGSEAERIKA QGAQQIQLMR QQLIRQLRTG
LGAEAVNKAA EIVRAHVADP QAQSATVDRF LSELEQMAPS SVVIDTAATS RLRAASRQSL
AALVEKFDSV AGGLDADGLT NLADELASVA KLLLSETALN KHLAEPTDDS APKVRLLERL
LSDKVSATTL DLLRTAVSNR WSTESNLIDA VEHTARLALL KRAEIAGEVD EVEEQLFRFG
RVLDAEPRLS ALLSDYTTPA EGRVALLDKA LTGRPGVNQT AAALLSQTVG LLRGERADEA
VIDLAELAVS RRGEVVAHVS AAAELSDAQR TRLTEVLSRI YGRPVSVQLH VDPELLGGLS
ITVGDEVIDG SIASRLAAAQ TGLPD
