ID A0A1H0S7X6_9CLOT Unreviewed; 427 AA.
AC A0A1H0S7X6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=H7E68_06405 {ECO:0000313|EMBL:MBB6714360.1},
GN SAMN04488529_104206 {ECO:0000313|EMBL:SDP37755.1};
OS Clostridium gasigenes.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=94869 {ECO:0000313|EMBL:SDP37755.1, ECO:0000313|Proteomes:UP000198597};
RN [1] {ECO:0000313|EMBL:SDP37755.1, ECO:0000313|Proteomes:UP000198597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12272 {ECO:0000313|EMBL:SDP37755.1,
RC ECO:0000313|Proteomes:UP000198597};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB6714360.1, ECO:0000313|Proteomes:UP000585258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM001 {ECO:0000313|EMBL:MBB6714360.1,
RC ECO:0000313|Proteomes:UP000585258};
RA Wambui J., Stevens M.J.A., Stephan R.;
RT "Clostridia isolated from Swiss meat.";
RL Submitted (AUG-2020) 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}.
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DR EMBL; JACKWY010000003; MBB6714360.1; -; Genomic_DNA.
DR EMBL; FNJM01000004; SDP37755.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0S7X6; -.
DR STRING; 94869.SAMN04488529_104206; -.
DR OrthoDB; 9767721at2; -.
DR Proteomes; UP000198597; Unassembled WGS sequence.
DR Proteomes; UP000585258; 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 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:UP000198597};
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"
SQ SEQUENCE 427 AA; 48001 MW; C494F6ED4BA14CCD CRC64;
MEAKMERIET NVVKFEVKVA AKEFQAALNK SYNKNAKNFN IPGFRKGKVP MAIVKQQYGI
EVLLEDAVNF AIDASYPQLL NENKINPVDY PQIEVITAEE GKDFVYTAQI TVYPEVKLGE
YKGLKIEKPS YEVTEEDVNA KLKETQEKSS RVEVKEDGII ENGNIAIIDF KGFVDGVAFD
GGEGSDYSLE IGSGSFIDTF ETQLVGAKSG DNVEVNVTFP ESYGKDELNG KDAKFEVTIK
EVKSKELPEL DDEFAKEVSE FDTLAQMKED IVKTMTEENA AKVKNEYEDA VINAVVENAT
IEVPTIMIEK EIDIMVKNLE TRLSQQGLTL EQYFQFTGTD AVKMREYMKE NAERKVRTDL
VLEAVEVAEK IEVSEEEIKV KAEEVAKMYA ADDASMVDLL IKNQRVALEV DIKTGKSIDF
LLENNKQ
//
