ATPF_MYCS2
ID ATPF_MYCS2 Reviewed; 170 AA.
AC A0R204; I7FR62;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=ATP synthase subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=ATP synthase F(0) sector subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=ATPase subunit I {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=F-type ATPase subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
DE Short=F-ATPase subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
GN Name=atpF {ECO:0000255|HAMAP-Rule:MF_01398};
GN OrderedLocusNames=MSMEG_4940, MSMEI_4813;
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].
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. {ECO:0000255|HAMAP-
CC Rule:MF_01398}.
CC -!- FUNCTION: Component of the F(0) channel, it forms part of the
CC peripheral stalk, linking F(1) to F(0). {ECO:0000255|HAMAP-
CC Rule:MF_01398}.
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 {ECO:0000255|HAMAP-Rule:MF_01398}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01398};
CC Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01398}.
CC -!- SIMILARITY: Belongs to the ATPase B chain family. {ECO:0000255|HAMAP-
CC Rule:MF_01398}.
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DR EMBL; CP000480; ABK73316.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP41258.1; -; Genomic_DNA.
DR RefSeq; WP_003896332.1; NZ_SIJM01000067.1.
DR RefSeq; YP_889192.1; NC_008596.1.
DR PDB; 7JG5; EM; 3.40 A; b=1-170.
DR PDB; 7JG6; EM; 3.70 A; b=1-170.
DR PDB; 7JG7; EM; 3.50 A; b=1-170.
DR PDB; 7JG8; EM; 3.30 A; b=1-170.
DR PDB; 7JG9; EM; 3.40 A; b=1-170.
DR PDB; 7JGA; EM; 3.20 A; b=1-170.
DR PDB; 7JGB; EM; 3.50 A; b=1-170.
DR PDB; 7JGC; EM; 3.40 A; b=1-170.
DR PDB; 7NJK; EM; 2.52 A; b=1-170.
DR PDB; 7NJL; EM; 2.71 A; b=1-170.
DR PDB; 7NJM; EM; 2.84 A; b=1-170.
DR PDB; 7NJN; EM; 2.64 A; b=1-170.
DR PDB; 7NJO; EM; 2.92 A; b=1-170.
DR PDB; 7NJP; EM; 2.84 A; b=1-170.
DR PDB; 7NJQ; EM; 2.67 A; b=1-170.
DR PDB; 7NJR; EM; 2.56 A; b=1-170.
DR PDB; 7NJS; EM; 2.46 A; b=1-170.
DR PDB; 7NJT; EM; 2.75 A; b=1-170.
DR PDB; 7NJU; EM; 3.74 A; b=1-170.
DR PDB; 7NJV; EM; 2.90 A; b=1-170.
DR PDB; 7NJW; EM; 3.67 A; b=1-170.
DR PDB; 7NJX; EM; 4.32 A; b=1-170.
DR PDB; 7NJY; EM; 2.94 A; b=1-170.
DR PDB; 7NK9; EM; 2.90 A; b=1-170.
DR PDB; 7NKD; EM; 3.12 A; b=1-170.
DR PDB; 7NKL; EM; 3.67 A; b=1-170.
DR PDB; 7NKP; EM; 4.06 A; b=1-170.
DR PDB; 7NKQ; EM; 2.98 A; b=1-170.
DR PDB; 7NL9; EM; 2.86 A; b=1-170.
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; A0R204; -.
DR SMR; A0R204; -.
DR STRING; 246196.MSMEI_4813; -.
DR PRIDE; A0R204; -.
DR EnsemblBacteria; ABK73316; ABK73316; MSMEG_4940.
DR EnsemblBacteria; AFP41258; AFP41258; MSMEI_4813.
DR GeneID; 66736262; -.
DR KEGG; msg:MSMEI_4813; -.
DR KEGG; msm:MSMEG_4940; -.
DR PATRIC; fig|246196.19.peg.4819; -.
DR eggNOG; COG0711; Bacteria.
DR OMA; VPPVMKV; -.
DR OrthoDB; 1999641at2; -.
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 InterPro; IPR028987; ATP_synth_B-like_membr_sf.
DR InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR InterPro; IPR005864; ATP_synth_F0_bsu_bac.
DR Pfam; PF00430; ATP-synt_B; 1.
DR SUPFAM; SSF81573; SSF81573; 1.
DR TIGRFAMs; TIGR01144; ATP_synt_b; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; Cell membrane; CF(0); Hydrogen ion transport;
KW Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..170
FT /note="ATP synthase subunit b"
FT /id="PRO_0000368599"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
FT REGION 121..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:7NL9"
FT HELIX 30..47
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 50..144
FT /evidence="ECO:0007829|PDB:7NJS"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 148..160
FT /evidence="ECO:0007829|PDB:7NJS"
SQ SEQUENCE 170 AA; 17621 MW; 96ACBCDB36818B87 CRC64;
MGEFSATILA ASQAAEEGGG GSNFLIPNGT FFAVLIIFLI VLGVISKWVV PPISKVLAER
EAMLAKTAAD NRKSAEQVAA AQADYEKEMA EARAQASALR DEARAAGRSV VDEKRAQASG
EVAQTLTQAD QQLSAQGDQV RSGLESSVDG LSAKLASRIL GVDVNSGGTQ
