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VATE_THET8
ID   VATE_THET8              Reviewed;         188 AA.
AC   P74901; Q5SIT8;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 2.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=V-type ATP synthase subunit E;
DE   AltName: Full=V-ATPase subunit E;
GN   Name=atpE; Synonyms=vatE; OrderedLocusNames=TTHA1276;
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10788522; DOI=10.1074/jbc.275.18.13955;
RA   Yokoyama K., Ohkuma S., Taguchi H., Yasunaga T., Wakabayashi T.,
RA   Yoshida M.;
RT   "V-type H+-ATPase/synthase from a thermophilic eubacterium, Thermus
RT   thermophilus. Subunit structure and operon.";
RL   J. Biol. Chem. 275:13955-13961(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA   Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane.
CC   -!- INTERACTION:
CC       P74901; Q5SIT5: TTHA1279; NbExp=4; IntAct=EBI-9016957, EBI-9016962;
CC   -!- SIMILARITY: Belongs to the V-ATPase E subunit family. {ECO:0000305}.
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DR   EMBL; D63799; BAA09870.1; -; Genomic_DNA.
DR   EMBL; AP008226; BAD71099.1; -; Genomic_DNA.
DR   RefSeq; WP_011228563.1; NC_006461.1.
DR   RefSeq; YP_144542.1; NC_006461.1.
DR   PDB; 3J0J; EM; 9.70 A; J/L=1-188.
DR   PDB; 3K5B; X-ray; 3.10 A; A/E=1-188.
DR   PDB; 3V6I; X-ray; 2.25 A; A/Y=2-188.
DR   PDB; 5GAR; EM; 6.40 A; G/H=3-188.
DR   PDB; 5GAS; EM; 9.50 A; G/H=3-188.
DR   PDB; 5TSJ; EM; 8.70 A; G/H=3-188.
DR   PDB; 5Y5X; EM; 5.00 A; J/L=1-188.
DR   PDB; 5Y5Y; EM; 4.70 A; J/L=1-188.
DR   PDB; 5Y5Z; EM; 6.70 A; J/L=1-188.
DR   PDB; 5Y60; EM; 7.50 A; J/L=1-188.
DR   PDB; 6LY9; EM; 3.93 A; L=1-188.
DR   PDB; 6QUM; EM; 3.25 A; J/L=1-188.
DR   PDB; 6R0W; EM; 3.60 A; J/L=1-188.
DR   PDB; 6R0Y; EM; 3.90 A; J/L=1-188.
DR   PDB; 6R0Z; EM; 3.80 A; J/L=1-188.
DR   PDB; 6R10; EM; 4.30 A; J/L=1-188.
DR   PDBsum; 3J0J; -.
DR   PDBsum; 3K5B; -.
DR   PDBsum; 3V6I; -.
DR   PDBsum; 5GAR; -.
DR   PDBsum; 5GAS; -.
DR   PDBsum; 5TSJ; -.
DR   PDBsum; 5Y5X; -.
DR   PDBsum; 5Y5Y; -.
DR   PDBsum; 5Y5Z; -.
DR   PDBsum; 5Y60; -.
DR   PDBsum; 6LY9; -.
DR   PDBsum; 6QUM; -.
DR   PDBsum; 6R0W; -.
DR   PDBsum; 6R0Y; -.
DR   PDBsum; 6R0Z; -.
DR   PDBsum; 6R10; -.
DR   AlphaFoldDB; P74901; -.
DR   SMR; P74901; -.
DR   DIP; DIP-58993N; -.
DR   IntAct; P74901; 1.
DR   STRING; 300852.55772658; -.
DR   TCDB; 3.A.2.2.1; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   EnsemblBacteria; BAD71099; BAD71099; BAD71099.
DR   GeneID; 3168454; -.
DR   KEGG; ttj:TTHA1276; -.
DR   PATRIC; fig|300852.9.peg.1255; -.
DR   eggNOG; COG1390; Bacteria.
DR   HOGENOM; CLU_123924_0_0_0; -.
DR   OMA; KPEWPEV; -.
DR   EvolutionaryTrace; P74901; -.
DR   Proteomes; UP000000532; Chromosome.
DR   GO; GO:0033178; C:proton-transporting two-sector ATPase complex, catalytic domain; IEA:InterPro.
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:InterPro.
DR   GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.2320.30; -; 1.
DR   HAMAP; MF_00311; ATP_synth_E_arch; 1.
DR   InterPro; IPR038495; ATPase_E_C.
DR   InterPro; IPR002842; ATPase_V1_Esu.
DR   Pfam; PF01991; vATP-synt_E; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP synthesis; Hydrogen ion transport; Ion transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..188
FT                   /note="V-type ATP synthase subunit E"
FT                   /id="PRO_0000117334"
FT   CONFLICT        38
FT                   /note="A -> D (in Ref. 1; BAA09870)"
FT                   /evidence="ECO:0000305"
FT   HELIX           3..93
FT                   /evidence="ECO:0007829|PDB:3V6I"
FT   HELIX           94..96
FT                   /evidence="ECO:0007829|PDB:3V6I"
FT   HELIX           100..114
FT                   /evidence="ECO:0007829|PDB:3V6I"
FT   STRAND          120..123
FT                   /evidence="ECO:0007829|PDB:3V6I"
FT   TURN            125..127
FT                   /evidence="ECO:0007829|PDB:3V6I"
FT   HELIX           128..138
FT                   /evidence="ECO:0007829|PDB:3V6I"
FT   STRAND          141..144
FT                   /evidence="ECO:0007829|PDB:3V6I"
FT   STRAND          150..155
FT                   /evidence="ECO:0007829|PDB:3V6I"
FT   STRAND          157..159
FT                   /evidence="ECO:0007829|PDB:3K5B"
FT   STRAND          162..166
FT                   /evidence="ECO:0007829|PDB:3V6I"
FT   HELIX           167..186
FT                   /evidence="ECO:0007829|PDB:3V6I"
SQ   SEQUENCE   188 AA;  20616 MW;  A6758A3A22200774 CRC64;
     MSKLEAILSQ EVEAEIQALL QEAEAKAEAV KREAEEKAKA LLQARERALE AQYRAALRRA
     ESAGELLVAT ARTQARGEVL EEVRRRVREA LEALPQKPEW PEVVRKLALE ALEALPGAKA
     LVANPEDLPH LEALARERGV ELQAEPALRL GVRAVGAEGK TQVENSLLAR LDRAWDALSS
     KVAQALWG
 
 
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