ID U5S941_9LACT Unreviewed; 426 AA.
AC U5S941;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 48.
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:AGY81789.1};
GN ORFNames=Q783_05795 {ECO:0000313|EMBL:AGY81789.1};
OS Carnobacterium inhibens subsp. gilichinskyi.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=1266845 {ECO:0000313|EMBL:AGY81789.1, ECO:0000313|Proteomes:UP000017469};
RN [1] {ECO:0000313|EMBL:AGY81789.1, ECO:0000313|Proteomes:UP000017469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WN1359 {ECO:0000313|EMBL:AGY81789.1,
RC ECO:0000313|Proteomes:UP000017469};
RX PubMed=24285647;
RA Leonard M.T., Panayotova N., Farmerie W.G., Triplett E.W., Nicholson W.L.;
RT "Complete Genome Sequence of Carnobacterium gilichinskyi Strain WN1359T
RT (DSM 27470T).";
RL Genome Announc. 1:e00985-13(2013).
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; CP006812; AGY81789.1; -; Genomic_DNA.
DR RefSeq; WP_023178046.1; NC_022606.1.
DR AlphaFoldDB; U5S941; -.
DR STRING; 1266845.Q783_05795; -.
DR KEGG; caw:Q783_05795; -.
DR PATRIC; fig|1266845.5.peg.1095; -.
DR eggNOG; COG0544; Bacteria.
DR HOGENOM; CLU_033058_3_2_9; -.
DR Proteomes; UP000017469; 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|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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00303};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00303};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|HAMAP-Rule:MF_00303}.
FT DOMAIN 162..247
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT COILED 254..284
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 426 AA; 47457 MW; BD71C790B2B9E678 CRC64;
MTANWEKKGT NDGVLTFEIS EEKIKEGLDT AFNKVKSTLS VPGFRKGKVP RAIFNKQFGE
EALYEDALNA VLPEAYDAAV VEAGIDPVAQ PKIDVKSMEK GEAWVIEAEV TVKPEVELGE
YKGLTVEKQD REVTDEDVEK NIEEKRAAQA ELVLKEDAAV EGDTVVIDYE GFKDGVAFEG
GKGENHSLEL GSNSFIPGFE EKLVGVKAED ELDVDLTFPE DYHAEDLKGA AVTFKVKVHE
VKAKELPALD DEFAKDVDEE VETLAELKEK IKTQLTDAKV ASAEEAVEEA AIRQAVDNAK
IEDLPWAMVH DEVHRQMDVF LNDMQRQGVS PEMYYQITGT TEQDLHKQME ADADLRTRTN
LVLEAIVEAE SFETSEDEVN EEIKNLAEQY GMDEKAVRAA LTPEMLKHDI SMKKAIDLIT
ETAKEQ
//
