(data stored in ACNUC29543 zone)

SWISSPROT: TIG_ACIBT

ID   TIG_ACIBT               Reviewed;         444 AA.
AC   A3M1Y6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   08-MAY-2019, entry version 81.
DE   RecName: Full=Trigger factor {ECO:0000255|HAMAP-Rule:MF_00303};
DE            Short=TF {ECO:0000255|HAMAP-Rule:MF_00303};
DE            EC=5.2.1.8 {ECO:0000255|HAMAP-Rule:MF_00303};
DE   AltName: Full=PPIase {ECO:0000255|HAMAP-Rule:MF_00303};
GN   Name=tig {ECO:0000255|HAMAP-Rule:MF_00303};
GN   OrderedLocusNames=A1S_0475;
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 /
OS   NCDC KC755 / 5377).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by
RT   high-density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(2007).
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:0000255|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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00303};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=About half TF is bound to
CC       the ribosome near the polypeptide exit tunnel while the other half
CC       is free in the cytoplasm. {ECO:0000255|HAMAP-Rule:MF_00303}.
CC   -!- DOMAIN: Consists of 3 domains; the N-terminus binds the ribosome,
CC       the middle domain has PPIase activity, while the C-terminus has
CC       intrinsic chaperone activity on its own. {ECO:0000255|HAMAP-
CC       Rule:MF_00303}.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. Tig subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00303}.
DR   EMBL; CP000521; ABO10930.2; -; Genomic_DNA.
DR   SMR; A3M1Y6; -.
DR   EnsemblBacteria; ABO10930; ABO10930; A1S_0475.
DR   KEGG; acb:A1S_0475; -.
DR   HOGENOM; HOG000218239; -.
DR   KO; K03545; -.
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; 1.10.3120.10; -; 1.
DR   Gene3D; 3.30.70.1050; -; 1.
DR   HAMAP; MF_00303; Trigger_factor_Tig; 1.
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   PANTHER; PTHR30560; PTHR30560; 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; SSF102735; SSF102735; 1.
DR   SUPFAM; SSF109998; SSF109998; 1.
DR   TIGRFAMs; TIGR00115; tig; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; A3M1Y6.
DR   SWISS-2DPAGE; A3M1Y6.
KW   Cell cycle; Cell division; Chaperone; Cytoplasm; Isomerase; Rotamase.
FT   CHAIN         1    444       Trigger factor.
FT                                /FTId=PRO_1000115493.
FT   DOMAIN      160    245       PPIase FKBP-type. {ECO:0000255|HAMAP-
FT                                Rule:MF_00303}.
SQ   SEQUENCE   444 AA;  49666 MW;  A1060184894C56B3 CRC64;
     MQVTTEAVSG VARRLNVSVP TSRINEQFEA RLKRTAKTVK INGFRPGKVP ANVVRREYGA
     SIYQEVVNDI IRDSVFEAIQ QEKINAVGMP NIEKVEHKED ALVFEATVEV YPEVEVKAFD
     GLEVERKTAE IKDADVDTMI ENLQKQRQTW AVTKGMAKKD MQVTFDFEGS IDGEKFEGGS
     AEDFKLVLGS GRMIPGFEDG IIGMKAGEEK VIDVTFPEDY QAENLAGKAA QFKITVKQVE
     KPKLPEIDAE FLKIFGVSEE EGIEKLKADV RKNMEREVRN GLRNQVKQAA FDALVAANEI
     EVPAAMVAQE IDRQRQQMVQ QFTQQFGGAG AQSFDKSMLP DELFKEQAER SVKLGVLVSK
     VLADAKLEVD QARVDAYIDD MASSYEDPTE VIEYFKNDAQ QRAQIEAVVL EDQVVDHILA
     SAKVTDKAVS YEDLLKEQQA RRMG
//

If you have problems or comments...

PBIL Back to PBIL home page