ID A0A1H7NCM8_9PROT Unreviewed; 434 AA.
AC A0A1H7NCM8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=SAMN05216387_106127 {ECO:0000313|EMBL:SEL21071.1};
OS Nitrosovibrio tenuis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosovibrio.
OX NCBI_TaxID=1233 {ECO:0000313|EMBL:SEL21071.1, ECO:0000313|Proteomes:UP000198620};
RN [1] {ECO:0000313|EMBL:SEL21071.1, ECO:0000313|Proteomes:UP000198620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nv1 {ECO:0000313|EMBL:SEL21071.1,
RC ECO:0000313|Proteomes:UP000198620};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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. {ECO:0000256|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;
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; FOBH01000006; SEL21071.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7NCM8; -.
DR STRING; 1233.SAMN05216387_106127; -.
DR OrthoDB; 9767721at2; -.
DR Proteomes; UP000198620; 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|HAMAP-Rule:MF_00303,
KW ECO:0000256|RuleBase:RU003914};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_00303,
KW ECO:0000256|RuleBase:RU003914};
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:UP000198620};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|HAMAP-Rule:MF_00303}.
FT DOMAIN 162..242
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 434 AA; 48783 MW; 09628E7765F6A371 CRC64;
MQSNVEELGA LERRLDVSIP QEKIETEVES RLKRLARTAK IHGFRPGKVP LKIVKQQYGP
QVRQEVIGDV LKKNFSDAVR EKNLRVAGYP RFEPKNIAEN ASQFEFSATF EVYPDVVLGD
LGATGVERPV VQVTQTDVDK TIETLRKQRV QYEPVGRPAA KGDRINIDFH GVIDGAEFAG
GNAENYSLVL GEGRLLKDFE EPLTDMSIGQ SKTFEVTFPG DYHGKEAAGK TATFDVKLNA
VEAPRLPEVD AEFARSLGVE EGDIQRLRGE IHANLEREVA NRIKARIKEQ VMQCLLDTTK
SQAPKALVEV ELERLMHDAR HDLASRGMNA KNVPLPHDLF YERAQRRVNL GLILAELVKM
HSLHPKPEQV RAMVEDLAQG YENPAEVVKW HYAAPDRLNE AESLALEDNV VQWVLEKVKV
EDKSMTLDEL MGRA
//
