TIG_ANAMM
ID TIG_ANAMM Reviewed; 441 AA.
AC Q5PBD1;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 89.
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=AM308;
OS Anaplasma marginale (strain St. Maries).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Anaplasma.
OX NCBI_TaxID=234826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=St. Maries;
RX PubMed=15618402; DOI=10.1073/pnas.0406656102;
RA Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L.,
RA Palmer G.H., McGuire T.C., Knowles D.P. Jr.;
RT "Complete genome sequencing of Anaplasma marginale reveals that the surface
RT is skewed to two superfamilies of outer membrane proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAV86398.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000030; AAV86398.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_035017828.1; NZ_AFMU01000046.1.
DR AlphaFoldDB; Q5PBD1; -.
DR SMR; Q5PBD1; -.
DR PRIDE; Q5PBD1; -.
DR KEGG; ama:AM308; -.
DR HOGENOM; CLU_033058_2_2_5; -.
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..441
FT /note="Trigger factor"
FT /id="PRO_0000179300"
FT DOMAIN 175..260
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00303"
SQ SEQUENCE 441 AA; 49286 MW; DEEA1769187B11E5 CRC64;
MQRFYVVKEV LSDKLKRVYE FTVGNEYLEQ QVDDRLREIA ANVRMDGFRK GKVSLDLVRR
NCGEDVVREV LSKVVDDASS QFMQEGGFGD VVTSEVRITS HPKVCSTEGK GGDLVYELQF
ELMPEVPSIN PEEIALKEME AEIGQEDVDK FIGELKTRYP NFVASDSPKQ RAAAGDKVVI
DYNSSFKGKA LRGGSAKGFV AVLGGGHLPK EFEDKITGMK VGDVKEFKLG FPSDYRVRLF
AGKEVEMSVK LVSIMVPKDV GDHEELAKSC GFGCAEDMVN FATESLKGRF AFMSDALMRK
ELFDHMETIY QGQVPESVVS QESARIRREL APSELEAMGE DGILKEAERR VRLGMLLMKV
SQDNNIAVEA RDISAFVQSN YLNYGASLES VLKLLRSNQG VRDHIRGKVL EDKVVRYMVA
KAKKERQNVP AGDLKSLFES I