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Database: UniProt
Entry: A0A1Y4RL64_9FIRM
LinkDB: A0A1Y4RL64_9FIRM
Original site: A0A1Y4RL64_9FIRM 
ID   A0A1Y4RL64_9FIRM        Unreviewed;       428 AA.
AC   A0A1Y4RL64;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Trigger factor {ECO:0000256|HAMAP-Rule:MF_00303, ECO:0000256|RuleBase:RU003914};
DE            Short=TF {ECO:0000256|HAMAP-Rule:MF_00303};
DE            EC=5.2.1.8 {ECO:0000256|HAMAP-Rule:MF_00303};
DE   AltName: Full=PPIase {ECO:0000256|HAMAP-Rule:MF_00303};
GN   Name=tig {ECO:0000256|HAMAP-Rule:MF_00303};
GN   ORFNames=B5E84_09710 {ECO:0000313|EMBL:OUQ17602.1};
OS   Lachnoclostridium sp. An14.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1965562 {ECO:0000313|EMBL:OUQ17602.1, ECO:0000313|Proteomes:UP000196089};
RN   [1] {ECO:0000313|Proteomes:UP000196089}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An14 {ECO:0000313|Proteomes:UP000196089};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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.
CC       {ECO:0000256|ARBA:ARBA00024849, ECO:0000256|HAMAP-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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000971, ECO:0000256|HAMAP-
CC         Rule:MF_00303, ECO:0000256|PROSITE-ProRule:PRU00277};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00303}.
CC       Note=About half TF is bound to the ribosome near the polypeptide exit
CC       tunnel while the other half is free in the cytoplasm.
CC       {ECO:0000256|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:0000256|HAMAP-Rule:MF_00303}.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. Tig subfamily.
CC       {ECO:0000256|ARBA:ARBA00005464, ECO:0000256|HAMAP-Rule:MF_00303,
CC       ECO:0000256|RuleBase:RU003914}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OUQ17602.1}.
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DR   EMBL; NFLE01000014; OUQ17602.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4RL64; -.
DR   OrthoDB; 9767721at2; -.
DR   Proteomes; UP000196089; Unassembled WGS sequence.
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; 3.10.50.40; -; 1.
DR   Gene3D; 3.30.70.1050; Trigger factor ribosome-binding domain; 1.
DR   Gene3D; 1.10.3120.10; Trigger factor, C-terminal domain; 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   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   Pfam; PF05697; Trigger_N; 1.
DR   PIRSF; PIRSF003095; Trigger_factor; 1.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR   SUPFAM; SSF102735; Trigger factor ribosome-binding domain; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_00303};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_00303};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00303};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00303};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00303};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196089};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|HAMAP-Rule:MF_00303}.
FT   DOMAIN          163..248
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
FT   COILED          261..295
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   428 AA;  47859 MW;  F72CF32EE6F8422B CRC64;
     MSLQVEKLEK NMAKLTVEVP AEKFIEAIGH AYKKNKNRFN VPGFRKGKVP QAMIEKMYGP
     EVFYEDAANE AIGQSYDAAA KESGLDIVSR PEIDLVQIEK GKDFIYTATV AVKPEVTLGQ
     YKGVEVEKAS AEVTDEDVEK ELKKVQEQNS RLVTVDDRAV QDGDQVVIDF DGYVDGEQFD
     GGKSEDYPLT IGSHTFIDTF EEQLIGKNAG EECEVNVTFP TEYHAAELAG KPAVFKVTVK
     EIKYKELPEL NDEFAGEVSE FETLEEYKAD VRAKLAEAKE KQAATENENR VVEAVVKNAT
     MEIPEPMIDA QLDNMVNEYA RNMQSHGISL DQYMQYTGMT IDKIKEQMRP QAVKRIETRL
     VLEAVAKAEN IQVSDEKVDE EIGKMAAAYK MEPEKLKGYM GEAEIASMKE DLAVQEAVDF
     LVAEAKLA
//
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