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Database: UniProt
Entry: G2KM07_MICAA
LinkDB: G2KM07_MICAA
Original site: G2KM07_MICAA 
ID   G2KM07_MICAA            Unreviewed;       454 AA.
AC   G2KM07;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 65.
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:AEP09703.1};
GN   OrderedLocusNames=MICA_1383 {ECO:0000313|EMBL:AEP09703.1};
OS   Micavibrio aeruginosavorus (strain ARL-13).
OC   Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC   Pseudobdellovibrionaceae; Micavibrio.
OX   NCBI_TaxID=856793 {ECO:0000313|EMBL:AEP09703.1, ECO:0000313|Proteomes:UP000009286};
RN   [1] {ECO:0000313|EMBL:AEP09703.1, ECO:0000313|Proteomes:UP000009286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARL-13 {ECO:0000313|EMBL:AEP09703.1,
RC   ECO:0000313|Proteomes:UP000009286};
RX   PubMed=21936919; DOI=10.1186/1471-2164-12-453;
RA   Wang Z., Kadouri D., Wu M.;
RT   "Genomic insights into an obligate epibiotic bacterial predator: Micavibrio
RT   aeruginosavorus ARL-13.";
RL   BMC Genomics 12:453-453(2011).
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; CP002382; AEP09703.1; -; Genomic_DNA.
DR   RefSeq; WP_014102926.1; NC_016026.1.
DR   AlphaFoldDB; G2KM07; -.
DR   STRING; 856793.MICA_1383; -.
DR   KEGG; mai:MICA_1383; -.
DR   eggNOG; COG0544; Bacteria.
DR   HOGENOM; CLU_033058_2_2_5; -.
DR   OMA; KGIKTQF; -.
DR   Proteomes; UP000009286; 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:UP000009286};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|HAMAP-Rule:MF_00303}.
FT   DOMAIN          163..247
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
FT   REGION          435..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   454 AA;  51244 MW;  EF943CC7771BDAD1 CRC64;
     MQVKELKKEG LSCQYEVTVT AQDIDAQVDV RLQEVGETIS LPGFRKGKVP LKLLKQKYGR
     SVMAEVIEKV VNDGAQKLIT EKNLRPALQP KFEVTSFDEG KDLTYTMAVE LLPEFKVTDV
     KAIKLVKPVV KADKKEIDET LERIAKSNAE YETITESRPT KKGDVIVMDF HGRTAKDNKP
     HPGMHAHGAK LELGSGQFIP GFEDQLVGKS VGDKVEVKVT FPEAYHAAEL SGQDAIFDVE
     IHEIQVAKDA KVDDDFAKKL GLDSEQALRD LVEKQIQSQY DDVSRMKLKR ALLDALDEAH
     DFELPQGMLD LEYNNILSQV RIERQGDLKD GKLELTTEEE DELRAIAARR VRLGLVLSEI
     GRENNIQITD QEMQRAVIME AQRFPGQEGE VFEYYRKNRQ ALEALRAPVF EDKVVDFLFE
     LADVSEKVVT VEELTKEDDT PYTGKKAEKA KKKA
//
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