(data stored in ACNUC7421 zone)

SWISSPROT: TIG_SYNFM

ID   TIG_SYNFM               Reviewed;         435 AA.
AC   A0LEF2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 74.
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};
GN   OrderedLocusNames=Sfum_0101;
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB;
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., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-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.
CC       {ECO:0000255|HAMAP-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
CC       the ribosome near the polypeptide exit tunnel while the other half
CC       is free in the cytoplasm. {ECO:0000255|HAMAP-Rule:MF_00303}.
CC   -!- DOMAIN: Consists of 3 domains; the N-terminus binds the ribosome,
CC       the middle domain has PPIase activity, while the C-terminus has
CC       intrinsic chaperone activity on its own. {ECO:0000255|HAMAP-
CC       Rule:MF_00303}.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. Tig subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00303}.
DR   EMBL; CP000478; ABK15804.1; -; Genomic_DNA.
DR   RefSeq; WP_011696977.1; NC_008554.1.
DR   SMR; A0LEF2; -.
DR   STRING; 335543.Sfum_0101; -.
DR   EnsemblBacteria; ABK15804; ABK15804; Sfum_0101.
DR   KEGG; sfu:Sfum_0101; -.
DR   eggNOG; ENOG4105DEA; Bacteria.
DR   eggNOG; COG0544; LUCA.
DR   KO; K03545; -.
DR   OMA; MAMIEDR; -.
DR   OrthoDB; 932993at2; -.
DR   BioCyc; SFUM335543:G1G7I-106-MONOMER; -.
DR   Proteomes; UP000001784; 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; 3.30.70.1050; -; 1.
DR   HAMAP; MF_00303; Trigger_factor_Tig; 1.
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.
PE   3: Inferred from homology;
DR   PRODOM; A0LEF2.
DR   SWISS-2DPAGE; A0LEF2.
KW   Cell cycle; Cell division; Chaperone; Complete proteome; Cytoplasm;
KW   Isomerase; Reference proteome; Rotamase.
FT   CHAIN         1    435       Trigger factor.
FT                                /FTId=PRO_1000022773.
FT   DOMAIN      163    248       PPIase FKBP-type. {ECO:0000255|HAMAP-
FT                                Rule:MF_00303}.
SQ   SEQUENCE   435 AA;  49942 MW;  B7EC36B351998195 CRC64;
     MNVSVVDLSE NQKKLQVEIP PEKVRQEIEG KYREMSRRIK IKGFRPGKVP RSIIKSYYGK
     TIEQEVSSQF IQETFPEALK ETDLKPLVEA DVSETHFNDS GSFSYTAIVD VCPPFELEGY
     RGLEIRKPSI DVADEQVDSE LQRLREQHAE LRTLETERPA REGDVAVIDF TPSVDGKVFE
     KGKSADYMAE IGKKAVHPDF DANLIGRRAG ETVSFEVDYP ENAPMREIAG KRVLFEVTVK
     EVKEKVLPEL DDDFAQAVNS RFDALDALKQ TIREELLKRE EYQARSDVQQ QILDQLLSKV
     KIELSAKVID REVDRMVGNL LHQFESQGLK MDVSKFNTPE IRADYRPQAE RNILRRLILE
     KIADQENLKL TDEEIEQVYQ EVARYARMDV ATVKHEFADS AVVEQSKESK IQEKVFRFLE
     SEAVSGHISQ EEKSE
//

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