位置:首页 > 蛋白库 > TIG_SHEDO
TIG_SHEDO
ID   TIG_SHEDO               Reviewed;         434 AA.
AC   Q12LA0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Trigger factor {ECO:0000255|HAMAP-Rule:MF_00303};
DE            Short=TF {ECO:0000255|HAMAP-Rule:MF_00303};
DE            EC=5.2.1.8 {ECO:0000255|HAMAP-Rule:MF_00303};
DE   AltName: Full=PPIase {ECO:0000255|HAMAP-Rule:MF_00303};
GN   Name=tig {ECO:0000255|HAMAP-Rule:MF_00303}; OrderedLocusNames=Sden_2496;
OS   Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS217 / ATCC BAA-1090 / DSM 15013;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of Shewanella denitrificans OS217.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in protein export. Acts as a chaperone by
CC       maintaining the newly synthesized protein in an open conformation.
CC       Functions as a peptidyl-prolyl cis-trans isomerase. {ECO:0000255|HAMAP-
CC       Rule:MF_00303}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00303};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=About half TF is bound to the
CC       ribosome near the polypeptide exit tunnel while the other half is free
CC       in the cytoplasm. {ECO:0000255|HAMAP-Rule:MF_00303}.
CC   -!- DOMAIN: Consists of 3 domains; the N-terminus binds the ribosome, the
CC       middle domain has PPIase activity, while the C-terminus has intrinsic
CC       chaperone activity on its own. {ECO:0000255|HAMAP-Rule:MF_00303}.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. Tig subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00303}.
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; CP000302; ABE55776.1; -; Genomic_DNA.
DR   RefSeq; WP_011496927.1; NC_007954.1.
DR   AlphaFoldDB; Q12LA0; -.
DR   SMR; Q12LA0; -.
DR   STRING; 318161.Sden_2496; -.
DR   EnsemblBacteria; ABE55776; ABE55776; Sden_2496.
DR   KEGG; sdn:Sden_2496; -.
DR   eggNOG; COG0544; Bacteria.
DR   HOGENOM; CLU_033058_2_0_6; -.
DR   OMA; KGIKTQF; -.
DR   OrthoDB; 932993at2; -.
DR   Proteomes; UP000001982; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.3120.10; -; 1.
DR   Gene3D; 3.10.50.40; -; 1.
DR   Gene3D; 3.30.70.1050; -; 1.
DR   HAMAP; MF_00303; Trigger_factor_Tig; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   InterPro; IPR005215; Trig_fac.
DR   InterPro; IPR008880; Trigger_fac_C.
DR   InterPro; IPR037041; Trigger_fac_C_sf.
DR   InterPro; IPR008881; Trigger_fac_ribosome-bd_bac.
DR   InterPro; IPR036611; Trigger_fac_ribosome-bd_sf.
DR   InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR   PANTHER; PTHR30560; PTHR30560; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   Pfam; PF05698; Trigger_C; 1.
DR   Pfam; PF05697; Trigger_N; 1.
DR   PIRSF; PIRSF003095; Trigger_factor; 1.
DR   SUPFAM; SSF102735; SSF102735; 1.
DR   SUPFAM; SSF109998; SSF109998; 1.
DR   TIGRFAMs; TIGR00115; tig; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Chaperone; Cytoplasm; Isomerase;
KW   Reference proteome; Rotamase.
FT   CHAIN           1..434
FT                   /note="Trigger factor"
FT                   /id="PRO_1000022754"
FT   DOMAIN          160..245
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00303"
SQ   SEQUENCE   434 AA;  47515 MW;  D1611F5002DFF8BD CRC64;
     MQVSVETTEG LGRRLTISVP AEQIEKMVKD GITREAKRAR LPGFRPGKVP LSEINKRYGQ
     AIRQDVMGEV MQRNFIEAII AEKLNPAGAP TFMPGKSVGE SFEFVATFEI YPEITLTGLD
     TIAVEQPKAE VNDADLDAMI ETLRKQHATF AVVERASAAG DKVKMNFVGS IDGEEFDGGK
     ADDFELEIGS NRMIPGFETG VTGHKAGETF DIEVSFPEDY HAENLKGKAA KFAITLTEVQ
     AAQLPEVNDE FATLFGITSG GVDALKAEIR KNMTRELEQA LKANVKEQVI NGLLAANDVT
     IPSALIDGEV EVLRKQAMQR FGGQTKNMPE LPAELFTEQA ERRVKIGLLL GEVIKTSELK
     AEDSRVQALI ASMASAYEDP AEVVAYYNSN KEMMQNMRNV ALEEQAVEAL LKSAKVTTKE
     VAFEEFMNKA SGRA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024