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Database: UniProt
Entry: A0A371BGT9_9SPHN
LinkDB: A0A371BGT9_9SPHN
Original site: A0A371BGT9_9SPHN 
ID   A0A371BGT9_9SPHN        Unreviewed;       502 AA.
AC   A0A371BGT9;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=DXH95_04740 {ECO:0000313|EMBL:RDV06717.1};
OS   Sphingorhabdus pulchriflava.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingorhabdus.
OX   NCBI_TaxID=2292257 {ECO:0000313|EMBL:RDV06717.1, ECO:0000313|Proteomes:UP000263833};
RN   [1] {ECO:0000313|Proteomes:UP000263833}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GY_G {ECO:0000313|Proteomes:UP000263833};
RA   Kim S.-J., Jung G.-Y.;
RL   Submitted (AUG-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.
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}.
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:RDV06717.1}.
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DR   EMBL; QRGP01000001; RDV06717.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A371BGT9; -.
DR   OrthoDB; 9767721at2; -.
DR   Proteomes; UP000263833; 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   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:UP000263833};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|HAMAP-Rule:MF_00303}.
FT   DOMAIN          164..244
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
FT   REGION          438..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..494
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   502 AA;  55227 MW;  05B003E5302110E5 CRC64;
     MQAQETQNEG LKRAYRLTVT VADIESRIDA EVQKIAPQVR MPGFRPGKVP ANLVKKMHKD
     ALLQEALNTS IQEGVQKTIT DNKLRPATQP HVHLDHDYAP GKDAVVDFHF EILPSIPEVK
     IEGLSLERLT VEAEGAEIDA ALERLASGHK NFETAAKSHK AATGDVVVID FEGKVDGVPF
     DGGKGEGMSV ELGSGQLIPG FEDQLVGVKA NDSKVIKVTF PDDYGAKELA GKAATFDIVV
     GEVKKPVESK ADDSLAQAFG LESLDKLKEL MKIQVEQELN GLTRTYMKRQ LLDQLAADHD
     FEVPPSMVEA EFEQIWSQLE QEADREEDPE AARKEMEAER EDYRDIAVRR VRLGLLLSEI
     GQGNGVEVSN QEMQMLVTQA SQQYRPEDRQ RFVQYLQENP MAAAQLRAPL FEDKVVDFLF
     DKAIVSEKTV TRAELEAAIE AEPEAKPSKK APAKKAAAKK EAVPAKEEKP AAKKAAPKKE
     AAKDEGEKPA KKAPAKKAAA KK
//
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