位置:首页 > 蛋白库 > ATPE_SALRD
ATPE_SALRD
ID   ATPE_SALRD              Reviewed;         149 AA.
AC   Q2RZV2;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=ATP synthase epsilon chain {ECO:0000255|HAMAP-Rule:MF_00530};
DE   AltName: Full=ATP synthase F1 sector epsilon subunit {ECO:0000255|HAMAP-Rule:MF_00530};
DE   AltName: Full=F-ATPase epsilon subunit {ECO:0000255|HAMAP-Rule:MF_00530};
GN   Name=atpC {ECO:0000255|HAMAP-Rule:MF_00530}; OrderedLocusNames=SRU_2430;
OS   Salinibacter ruber (strain DSM 13855 / M31).
OC   Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC   Rhodothermaceae; Salinibacter.
OX   NCBI_TaxID=309807;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13855 / CECT 5946 / M31;
RX   PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA   Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H.,
RA   Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA   Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA   Legault B., Rodriguez-Valera F.;
RT   "The genome of Salinibacter ruber: convergence and gene exchange among
RT   hyperhalophilic bacteria and archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. {ECO:0000255|HAMAP-Rule:MF_00530}.
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, b and c.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00530}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00530}.
CC   -!- SIMILARITY: Belongs to the ATPase epsilon chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00530}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000159; ABC44149.1; -; Genomic_DNA.
DR   RefSeq; WP_011405147.1; NC_007677.1.
DR   RefSeq; YP_446529.1; NC_007677.1.
DR   AlphaFoldDB; Q2RZV2; -.
DR   SMR; Q2RZV2; -.
DR   STRING; 309807.SRU_2430; -.
DR   PRIDE; Q2RZV2; -.
DR   EnsemblBacteria; ABC44149; ABC44149; SRU_2430.
DR   GeneID; 61497217; -.
DR   KEGG; sru:SRU_2430; -.
DR   PATRIC; fig|309807.25.peg.2532; -.
DR   eggNOG; COG0355; Bacteria.
DR   HOGENOM; CLU_084338_1_1_10; -.
DR   OMA; MGGFAEI; -.
DR   Proteomes; UP000008674; 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   CDD; cd12152; F1-ATPase_delta; 1.
DR   Gene3D; 2.60.15.10; -; 1.
DR   HAMAP; MF_00530; ATP_synth_epsil_bac; 1.
DR   InterPro; IPR001469; ATP_synth_F1_dsu/esu.
DR   InterPro; IPR020547; ATP_synth_F1_dsu/esu_C.
DR   InterPro; IPR020546; ATP_synth_F1_dsu/esu_N.
DR   InterPro; IPR036771; ATPsynth_dsu/esu_N.
DR   PANTHER; PTHR13822; PTHR13822; 1.
DR   Pfam; PF00401; ATP-synt_DE; 1.
DR   Pfam; PF02823; ATP-synt_DE_N; 1.
DR   SUPFAM; SSF51344; SSF51344; 1.
DR   TIGRFAMs; TIGR01216; ATP_synt_epsi; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Cell inner membrane; Cell membrane; CF(1);
KW   Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW   Transport.
FT   CHAIN           1..149
FT                   /note="ATP synthase epsilon chain"
FT                   /id="PRO_0000265885"
FT   REGION          99..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..138
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   149 AA;  16440 MW;  C29F313D2C5C98C1 CRC64;
     MADELTVDIV TPDERSFQGP ANGVRAPGIE GSFEVREDHA PMIAAFGIGP LIVKTQAAHE
     YADMHNDRII FATSGGFLEV IDNKVTVLAE TVEPASEIDV ERAESAEERA KRRLEEGVQE
     EERETHEAAR DRARNRLRVA MGKVGTRQS
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024