TIG_HELPJ
ID TIG_HELPJ Reviewed; 451 AA.
AC Q9ZL49;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Trigger factor;
DE Short=TF;
DE EC=5.2.1.8;
DE AltName: Full=PPIase;
GN Name=tig; OrderedLocusNames=jhp_0731;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
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 (By similarity).
CC {ECO:0000250}.
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;
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:0000250}.
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:0000250}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. Tig subfamily.
CC {ECO:0000305}.
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DR EMBL; AE001439; AAD06304.1; -; Genomic_DNA.
DR PIR; A71896; A71896.
DR RefSeq; WP_001047759.1; NZ_CP011330.1.
DR AlphaFoldDB; Q9ZL49; -.
DR SMR; Q9ZL49; -.
DR STRING; 85963.jhp_0731; -.
DR EnsemblBacteria; AAD06304; AAD06304; jhp_0731.
DR KEGG; hpj:jhp_0731; -.
DR PATRIC; fig|85963.30.peg.245; -.
DR eggNOG; COG0544; Bacteria.
DR OMA; KGIKTQF; -.
DR Proteomes; UP000000804; 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; Rotamase.
FT CHAIN 1..451
FT /note="Trigger factor"
FT /id="PRO_0000179364"
FT DOMAIN 165..250
FT /note="PPIase FKBP-type"
SQ SEQUENCE 451 AA; 51805 MW; A2CAB93105A2F740 CRC64;
MNLEVKKIDT ANARLSAKPS IEDLEKRYDK IAQKIAQKVK IDGFRRGKVP LSLVKTRYQA
QIEQDAQEEM IQEVLKNALK ELGVETKDLI GSPNFTKFEK KDTHFEIEAD IGLKPTIVLD
KIQECVPSVG VEVPNEEKVN ERLKQLAKDY AKFVDTDSQR KAQNDDKLTI DFEGFIDNAP
FEGGKAENFS LILGSKQMLE DFEKALLGMQ ASEEKEFPLT FPSGYHAEHL AGKEALFKVK
LRQIQVREAL EINDELAKIV LANEENATLE LLKERVKGQL FLENKARLYN EELKEKLIEN
LDEKILFDLP KTIIEQEMDL LFRNALYSMQ AEEVKSLQDS QEKAKEKRES FRNDATKSVK
ITFVIDALAK EEKIGVHDNE VFQTLYYEAM MTGQNPENLI EQYRKNNMLA AVKMAMIEDR
VLAYLLDKNL PKEQQEILEK MRPNAQKTQV G
