TIG_DESAL
ID TIG_DESAL Reviewed; 438 AA.
AC B8FA61;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 71.
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=Dalk_1457;
OS Desulfatibacillum aliphaticivorans.
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulfatibacillum.
OX NCBI_TaxID=218208;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK-01;
RX PubMed=21651686; DOI=10.1111/j.1462-2920.2011.02516.x;
RA Callaghan A.V., Morris B.E., Pereira I.A., McInerney M.J., Austin R.N.,
RA Groves J.T., Kukor J.J., Suflita J.M., Young L.Y., Zylstra G.J., Wawrik B.;
RT "The genome sequence of Desulfatibacillum alkenivorans AK-01: a blueprint
RT for anaerobic alkane oxidation.";
RL Environ. Microbiol. 14:101-113(2012).
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}.
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DR EMBL; CP001322; ACL03157.1; -; Genomic_DNA.
DR RefSeq; WP_012610592.1; NC_011768.1.
DR AlphaFoldDB; B8FA61; -.
DR SMR; B8FA61; -.
DR PRIDE; B8FA61; -.
DR EnsemblBacteria; ACL03157; ACL03157; Dalk_1457.
DR KEGG; dal:Dalk_1457; -.
DR eggNOG; COG0544; Bacteria.
DR HOGENOM; CLU_033058_3_2_7; -.
DR OMA; KGIKTQF; -.
DR OrthoDB; 932993at2; -.
DR Proteomes; UP000000739; 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..438
FT /note="Trigger factor"
FT /id="PRO_1000119513"
FT DOMAIN 163..249
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00303"
SQ SEQUENCE 438 AA; 50892 MW; 045DC109D904589C CRC64;
MQVTVEDLSS VKKVLHIEAP AEDVKKALDS AYAELKKQAK VKGFRPGKAP RSVLERLYKS
DVESDVAGEI ISDAFRDAIM ETKLKIVGPP EIEPPAIVSD EPYKFDATVE IFPELSDLNL
KEIELSKNMY KATEQEIENQ IAMIRKNMSS LETEEEDRPA KEEDFVLIDY EGVCPDGQPD
ELRFTENFTM ELGTGRILKD FDAQIVGMKR DEEKDFEISF PEDYFNKELA SKQVKFHVKL
KEIRKQILPE LDDEFAKDLG EYETLDQLKD SIRDHLQQGY DRRSEQELDE QVFQALLNRV
EFEVPETLIK HETASMVSEA ERALSYRDMT FEDTGATKED MEERYREPAE QQVRRYLLLD
KIVEQENVEL PEEELENAFK GMAESLRQPL EIVKKYYASD AEQMNMLRQT LLQKEALKYV
KNLNEIKEVE LELQETEE
