ID D4K140_9FIRM Unreviewed; 325 AA.
AC D4K140;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Trigger factor {ECO:0000256|ARBA:ARBA00016902};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
DE AltName: Full=PPIase {ECO:0000256|ARBA:ARBA00029986};
GN ORFNames=FP2_26840 {ECO:0000313|EMBL:CBK99989.1};
OS Faecalibacterium prausnitzii L2-6.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Faecalibacterium.
OX NCBI_TaxID=718252 {ECO:0000313|EMBL:CBK99989.1, ECO:0000313|Proteomes:UP000008804};
RN [1] {ECO:0000313|EMBL:CBK99989.1, ECO:0000313|Proteomes:UP000008804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L2-6 {ECO:0000313|Proteomes:UP000008804};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Faecalibacterium prausnitzii L2/6.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBK99989.1, ECO:0000313|Proteomes:UP000008804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L2-6 {ECO:0000313|Proteomes:UP000008804};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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;
CC Evidence={ECO:0000256|ARBA:ARBA00000971};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; FP929045; CBK99989.1; -; Genomic_DNA.
DR AlphaFoldDB; D4K140; -.
DR STRING; 718252.FP2_26840; -.
DR KEGG; fpr:FP2_26840; -.
DR PATRIC; fig|718252.3.peg.877; -.
DR eggNOG; COG0544; Bacteria.
DR HOGENOM; CLU_033058_3_2_9; -.
DR BioCyc; FPRA718252:G1375-2309-MONOMER; -.
DR Proteomes; UP000008804; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
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:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:InterPro.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 1.10.3120.10; Trigger factor, C-terminal domain; 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; IPR027304; Trigger_fact/SurA_dom_sf.
DR NCBIfam; TIGR00115; tig; 1.
DR PANTHER; PTHR30560; TRIGGER FACTOR CHAPERONE AND PEPTIDYL-PROLYL CIS/TRANS ISOMERASE; 1.
DR PANTHER; PTHR30560:SF3; TRIGGER FACTOR-LIKE PROTEIN TIG, CHLOROPLASTIC; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR Pfam; PF05698; Trigger_C; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
PE 4: Predicted;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Reference proteome {ECO:0000313|Proteomes:UP000008804};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110}.
FT DOMAIN 50..131
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|Pfam:PF00254"
FT DOMAIN 154..309
FT /note="Trigger factor C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05698"
SQ SEQUENCE 325 AA; 36360 MW; 18DC2EC56D1A395C CRC64;
MDKKNTPEVK LGQYKGLAVT RHVRPVTDKT VDIELVHQAR MHAVYHPTTE PAKRGFRALL
DFAGYMDGRE IPDSRMEKVM VVLGDGKLMP AAEQAIYGHR AGEVFRFDFT YPQDFRLPEL
SGKTAQFEIE LRSLAEKITP APDEAFAKSL GFDSLDALKA DLRAKKQKIH EEGADRAAGK
QLLDMAGANM TVDLPAEILD RTAQNEMKLL KERLSRSGIT LEQHCKNSRT TPEALEKDYR
AQAESRIRFV LAAKAIAEAE NIVVHPEEVN AEYRRLSQLQ DTPEAEIRKA LPEDTIAAAL
AAKKVQRFLL DNAQVTTVTD APEKE
//
