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Database: UniProt
Entry: A0A2C9SUJ7_9MYCO
LinkDB: A0A2C9SUJ7_9MYCO
Original site: A0A2C9SUJ7_9MYCO 
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
//
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