TIG_BRUA4
ID TIG_BRUA4 Reviewed; 477 AA.
AC A6X192;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 83.
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=Oant_2280;
OS Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 /
OS LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37) (Ochrobactrum anthropi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=439375;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 / NBRC
RC 15819 / NCTC 12168 / Alc 37;
RX PubMed=21685287; DOI=10.1128/jb.05335-11;
RA Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M.,
RA Ugalde R.A., Garcia E., Tolmasky M.E.;
RT "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic
RT pathogen and symbiont of several eukaryotic hosts.";
RL J. Bacteriol. 193:4274-4275(2011).
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=ABS14996.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000758; ABS14996.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A6X192; -.
DR SMR; A6X192; -.
DR STRING; 439375.Oant_2280; -.
DR EnsemblBacteria; ABS14996; ABS14996; Oant_2280.
DR KEGG; oan:Oant_2280; -.
DR PATRIC; fig|439375.7.peg.2400; -.
DR eggNOG; COG0544; Bacteria.
DR HOGENOM; CLU_033058_2_2_5; -.
DR PhylomeDB; A6X192; -.
DR Proteomes; UP000002301; Chromosome 1.
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..477
FT /note="Trigger factor"
FT /id="PRO_0000322447"
FT DOMAIN 169..254
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00303"
FT REGION 435..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 477 AA; 53432 MW; D29B888CA1145837 CRC64;
MQVTETLNEG LKREIKVVVP AKDLEAKLAE RLETARDRAK INGFRPGKVP AAHLRKMYGK
SFMAEIVNEI LNDSSRSLLA ERNEKSATQP EVIMSEDEKE AEQVLDGKAD FVFSLNYEVL
PAIEVKDFSK IAVTREVVDI SDEEVDDQVK RIASSTRAFE TKKGKAENED RVTIDYLGKL
DGEPFEGGAD NDAQLVLGSG QFIPGFEEQL VGVKAGDEKV ITVTFPAEYG AAHLAGKEAT
FDITVKEVAK PNELVLDDET AKKLGIESLE RLRQVVREQI ESQYGQITRQ KVKRQILDAL
DGDYQFATPQ KLVDAEFNNI WQQINFDLQQ AGRTFEDEET TEEAAREEYR KLAERRVRLG
LVLSEIGEKA GVEVSEEELQ RAVYDQVRRY PGQEKEIYEF LRKTPDAVAN LRAPIFEEKV
VDHLLANISV TDKKVSKEEL TAEDEDAASE AKPAKKAAPK KKAAPKKKAD EGKSEEA
