ID A0A2C9SUJ7_9MYCO Unreviewed; 472 AA.
AC A0A2C9SUJ7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-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 ECO:0000313|EMBL:GAY15399.1};
GN ORFNames=MSZK_21250 {ECO:0000313|EMBL:GAY15399.1};
OS Mycobacterium sp. shizuoka-1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=2039281 {ECO:0000313|EMBL:GAY15399.1, ECO:0000313|Proteomes:UP000223528};
RN [1] {ECO:0000313|EMBL:GAY15399.1, ECO:0000313|Proteomes:UP000223528}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=shizuoka-1 {ECO:0000313|Proteomes:UP000223528};
RA Yoshida M., Izumiyama S., Fukano H., Sugiyama K., Suzuki M., Shibayama K.,
RA Hoshino Y.;
RT "Draft genome sequence of Mycobacterium sp. shizuoka-1.";
RL Submitted (OCT-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. {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}.
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:GAY15399.1}.
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DR EMBL; BEWG01000031; GAY15399.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C9SUJ7; -.
DR OrthoDB; 9767721at2; -.
DR Proteomes; UP000223528; 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:UP000223528};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|HAMAP-Rule:MF_00303}.
FT DOMAIN 162..210
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REGION 435..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..462
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 472 AA; 51287 MW; F99184DA9B6698B4 CRC64;
MKSTVEKLSP TRVRINVEVP FTELQPDFDR AYKELAKQVR LPGFRPGKAP AKLLEARIGR
GAVLEQVVND ALPSRYSEAV VATEVTPLGQ PEIEVTKIED GEELVFTAEV DVRPDIELPD
LSSLKISVEP IEINDEEVDA ELESLRARFG TLKGVERPAQ TGDFVSIDLS ATVNGEELPD
AATEGLSHEV GSGQLIDGLD EAIVGLAEGE SKVFTTKLAA GEHAGEEAEV TVTVKSIKER
ELPEADDEFA QLASEFDTIE ELRENLVEQV KRVKRIHQAE KIRDNALELL LETTEVPLPE
AIVQAQVDQT VHNAIHGLDH DEAKFAEALE AEGSSREKFD AETREAAEKA VKTQLLMDAI
ADDLDIQVGQ NDLTERLVLM SRQYGIEPAQ LLQILQQNNQ LPAMFADVRR GLTVAAVVEA
ATVTDTDGNV VDTAEFFGPP AEEDGAEAAE GDTDDASDEA GEAAEQQADK AE
//