TIG_BORAP
ID TIG_BORAP Reviewed; 452 AA.
AC Q0SMP7; G0IQG0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 95.
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};
GN OrderedLocusNames=BAPKO_0646, BafPKo_0630;
OS Borreliella afzelii (strain PKo) (Borrelia afzelii).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=390236;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PKo;
RX PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J.,
RA Wilske B., Platzer M.;
RT "Comparative genome analysis: selection pressure on the Borrelia vls
RT cassettes is essential for infectivity.";
RL BMC Genomics 7:211-211(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PKo;
RX PubMed=22123755; DOI=10.1128/jb.05951-11;
RA Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J.,
RA Fraser-Liggett C.M., Schutzer S.E.;
RT "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT Lyme disease agent isolates.";
RL J. Bacteriol. 193:6995-6996(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=AEL69830.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000395; ABH01881.1; -; Genomic_DNA.
DR EMBL; CP002933; AEL69830.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011601123.1; NC_017238.1.
DR AlphaFoldDB; Q0SMP7; -.
DR SMR; Q0SMP7; -.
DR STRING; 390236.BafPKo_0630; -.
DR PRIDE; Q0SMP7; -.
DR EnsemblBacteria; AEL69830; AEL69830; BafPKo_0630.
DR KEGG; baf:BAPKO_0646; -.
DR KEGG; bafz:BafPKo_0630; -.
DR PATRIC; fig|390236.22.peg.603; -.
DR eggNOG; COG0544; Bacteria.
DR HOGENOM; CLU_033058_3_1_12; -.
DR OMA; KGIKTQF; -.
DR OrthoDB; 932993at2; -.
DR Proteomes; UP000005216; 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; 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; 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.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Chaperone; Cytoplasm; Isomerase; Rotamase.
FT CHAIN 1..452
FT /note="Trigger factor"
FT /id="PRO_1000022648"
FT DOMAIN 170..256
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00303"
SQ SEQUENCE 452 AA; 52842 MW; E255F27E77B31DBE CRC64;
MILSKDIRLL PGSKVEAVIR VSKNIIQEKY NSLLQDYSSR LKIQGFRIGK VPISIIEKKY
SEGLRATVLE EVINNSLKEF FKEEPKRPLS YASPTIKEEN LRLNLDKDFE FTFVYETYPE
FKVPNIDDID IKVEVPEVFI DDSDIDNEIK SLQIENSIII EDEEGVVKKD SIVKVDFVEL
DDLLNEIVST KRQDFVFTVG KSETYYDFDR DVIGMRINEE RVIEKSYITD YKFEELAGSL
KKLKIKIKSI KKRDLPLIDD EFAKDISERY NTLDDLKNFI RSKILSLVEE KKEALKLNKF
FSTISEKLEI DIPRSMIEAE IEIAFKDAKR QNKMSLEEFK SMFYSSGYNG SDSLKDEILS
NLKSKLIIQK MVDLDPIKVT ENDLKDEMVR QSENSGVSYE EIKKFYEDQN LIFYLKDDIK
RKIVEKKILA SLKEVKGKQV SFKDFVNYKI CE
