位置:首页 > 蛋白库 > VATE_CHLTB
VATE_CHLTB
ID   VATE_CHLTB              Reviewed;         208 AA.
AC   B0BBU1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=V-type proton ATPase subunit E {ECO:0000255|HAMAP-Rule:MF_00311};
DE   AltName: Full=V-ATPase subunit E {ECO:0000255|HAMAP-Rule:MF_00311};
GN   Name=atpE {ECO:0000255|HAMAP-Rule:MF_00311}; OrderedLocusNames=CTLon_0558;
OS   Chlamydia trachomatis serovar L2b (strain UCH-1/proctitis).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=471473;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCH-1/proctitis;
RX   PubMed=18032721; DOI=10.1101/gr.7020108;
RA   Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA   Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA   Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT   "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT   venereum isolates.";
RL   Genome Res. 18:161-171(2008).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. {ECO:0000255|HAMAP-Rule:MF_00311}.
CC   -!- SIMILARITY: Belongs to the V-ATPase E subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_00311}.
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; AM884177; CAP06956.1; -; Genomic_DNA.
DR   RefSeq; WP_009873715.1; NC_010280.2.
DR   AlphaFoldDB; B0BBU1; -.
DR   SMR; B0BBU1; -.
DR   KEGG; ctl:CTLon_0558; -.
DR   HOGENOM; CLU_1314973_0_0_0; -.
DR   OMA; MQFEVKD; -.
DR   Proteomes; UP000000794; 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   HAMAP; MF_00311; ATP_synth_E_arch; 1.
DR   InterPro; IPR028987; ATP_synth_B-like_membr_sf.
DR   InterPro; IPR002842; ATPase_V1_Esu.
DR   InterPro; IPR009335; T3SS_HrpE/ATPase_suE.
DR   Pfam; PF06188; HrpE; 1.
DR   SUPFAM; SSF81573; SSF81573; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Hydrogen ion transport; Ion transport; Transport.
FT   CHAIN           1..208
FT                   /note="V-type proton ATPase subunit E"
FT                   /id="PRO_1000115672"
SQ   SEQUENCE   208 AA;  22946 MW;  36DA2728A17D4A23 CRC64;
     MADLSAQDKL KQICDALREE TLKPAEEEAG SIVHNAREQA KRIVEEAKEE AQRIIRSAEE
     TADQTLKKGE AALVQAGKRS LENLKQAVET KIFRESLGEW LDHVATDPEV SAKLVQALVQ
     AVDAQGISGN LSAYIGKHVS ARAVNEALGK EITSKLKEKG VSVGKFSGGA QLKVEERNWV
     LDMSSEVLLD LLTRFLQKDF REMIFQSC
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024