TIG_MYCGA
ID TIG_MYCGA Reviewed; 443 AA.
AC Q7NBA6;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 97.
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=MYCGA3730;
GN ORFNames=MGA_1297;
OS Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS (Mycoplasmoides gallisepticum).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=710127;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R(low / passage 15 / clone 2);
RX PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT "The complete genome sequence of the avian pathogen Mycoplasma
RT gallisepticum strain R(low).";
RL Microbiology 149:2307-2316(2003).
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; AE015450; AAP56723.2; -; Genomic_DNA.
DR RefSeq; WP_011113619.1; NC_004829.2.
DR AlphaFoldDB; Q7NBA6; -.
DR SMR; Q7NBA6; -.
DR KEGG; mga:MGA_1297; -.
DR PATRIC; fig|233150.7.peg.418; -.
DR HOGENOM; CLU_033058_3_2_14; -.
DR OMA; KGIKTQF; -.
DR OrthoDB; 932993at2; -.
DR Proteomes; UP000001418; 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..443
FT /note="Trigger factor"
FT /id="PRO_0000179381"
FT DOMAIN 169..254
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00303"
SQ SEQUENCE 443 AA; 51289 MW; 9CA15B02545591B1 CRC64;
MFKIREKTNA DHKVKYIVDV NEKNWNEAYQ KKLNAAVKNV KIQGFRKGHV PYQEAIKHID
QIGLFDRAVN QLVQPIYLEL VKQEKIKDSE TVLEENPEVS VVEIDDKKLA LSYSFETIPE
VKVGDYLKIN GFLSETPVKD EDVQTELVRI FKSAGKLVDK KEGATLEKGD IAFLDFSGEI
DNKAFEGGKA KNYELEIGSN SFIPGFEDQM VGMKVGEKRD LNLTFPKDYH EKTYAGKPVL
FKVKLNSIKE VQLPEMTVEK LNELMKTQYK NLDEAKEDIK KRMDRNQQEH ANQMNTMLLT
QFANEDCQFS HIPKSLLDRE VNLLYQQFAN QMQQIKMSVE DALKIQNQTK EQLYQRLTEQ
ATRAIKLVLV LEEIGDLEKI SVSEAEINQE IEERIKEISN NQELPKEQYD AIKNYFVTQK
ELIESMLTNK KVVDLIIKKN LAR
