ID A0A3G6ZMQ5_9MICO Unreviewed; 477 AA.
AC A0A3G6ZMQ5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=DT073_10570 {ECO:0000313|EMBL:AZC14099.1};
OS Microbacterium sp. ABRD28.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=2268461 {ECO:0000313|EMBL:AZC14099.1, ECO:0000313|Proteomes:UP000280903};
RN [1] {ECO:0000313|EMBL:AZC14099.1, ECO:0000313|Proteomes:UP000280903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ABRD_28 {ECO:0000313|EMBL:AZC14099.1};
RA Jin H.M.;
RT "Genome sequence of Microbacterium sp. ABRD28.";
RL Submitted (JUL-2018) 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; CP031015; AZC14099.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G6ZMQ5; -.
DR OrthoDB; 9767721at2; -.
DR Proteomes; UP000280903; Chromosome.
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:UP000280903};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|HAMAP-Rule:MF_00303}.
FT DOMAIN 167..214
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REGION 450..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 477 AA; 51717 MW; BF0E30B5F2D002E7 CRC64;
MVTTTVEKLS PTRVKLRIAV SPEELKPSIT HAYEHIAQDV QIPGFRKGKV PAPIIDQRVG
RTAVLEHAVS EGLDAFYREA VTASEIRVMG RPSADVVEWP DAKDFSGDLL VDVEVDVRPE
FDLPDFEGTT IEVDAVEVDE SAVDAELDKL RSRFGTLVTV DRPAATGDFV ELDLVATIDG
NEVDRADGVS YEVGSGELLE GIDEAVDSLT AGEETTFRST LIGGDNAGQE AEVAVTVKAV
KERELPEADD DFAQMASEFD TIAELRDSLR ERAGEQSVFT QGSAARDKLI ETLLAGAEIP
VPQQLIEDEV HNHLEGEGRL EDDVHRAEVT EASEKQFRTQ MLLDAIVEKY EVQVSQDELT
QYLIQSSAQY GMSPQDFINA LQQGNQLPAM VGEVARNKAL AVALGKVTVV DTNGKTVDLT
GFVALEDEET AEDEVVEEAE DIADAAAEAD EVIAAEEAEA PKKPARKSRA KKADAAE
//
