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IF2_CHLTB
ID   IF2_CHLTB               Reviewed;         896 AA.
AC   B0BB83;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CTLon_0347;
OS   Chlamydia trachomatis serovar L2b (strain UCH-1/proctitis).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=471473;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCH-1/proctitis;
RX   PubMed=18032721; DOI=10.1101/gr.7020108;
RA   Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA   Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA   Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT   "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT   venereum isolates.";
RL   Genome Res. 18:161-171(2008).
CC   -!- FUNCTION: One of the essential components for the initiation of protein
CC       synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis
CC       and promotes its binding to the 30S ribosomal subunits. Also involved
CC       in the hydrolysis of GTP during the formation of the 70S ribosomal
CC       complex. {ECO:0000255|HAMAP-Rule:MF_00100}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00100}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00100}.
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DR   EMBL; AM884177; CAP06745.1; -; Genomic_DNA.
DR   RefSeq; WP_009873552.1; NC_010280.2.
DR   AlphaFoldDB; B0BB83; -.
DR   SMR; B0BB83; -.
DR   KEGG; ctl:CTLon_0347; -.
DR   HOGENOM; CLU_006301_3_1_0; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000000794; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd03702; IF2_mtIF2_II; 1.
DR   Gene3D; 3.40.50.10050; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00100_B; IF_2_B; 1.
DR   InterPro; IPR044145; IF2_II.
DR   InterPro; IPR006847; IF2_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR000178; TF_IF2_bacterial-like.
DR   InterPro; IPR015760; TIF_IF2.
DR   InterPro; IPR023115; TIF_IF2_dom3.
DR   InterPro; IPR036925; TIF_IF2_dom3_sf.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   PANTHER; PTHR43381; PTHR43381; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF11987; IF-2; 1.
DR   Pfam; PF04760; IF2_N; 1.
DR   SUPFAM; SSF50447; SSF50447; 2.
DR   SUPFAM; SSF52156; SSF52156; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00487; IF-2; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
DR   PROSITE; PS01176; IF2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..896
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000093772"
FT   DOMAIN          401..570
FT                   /note="tr-type G"
FT   REGION          32..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          410..417
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          435..439
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          456..459
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          510..513
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          546..548
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        33..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        119..134
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..165
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..254
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..274
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         410..417
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         456..460
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         510..513
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   896 AA;  97378 MW;  345BA0E5ED81170D CRC64;
     MEKAKLTKNL KLKIKNAQLT KAAGLDKLKQ KLAQAGSSDT KNSPASKAQT KEKSSKKTAG
     TPAPAPEVDL GATESTARRI RAKDRSSFAA EPTVTTALPG DASHLTLDAI PAIKAPEITS
     VTQKEQTLRE CTDTSSVQQE EKKESSEETS PETPERIEET PIIRTRTEPK SVVSIKPKFG
     PTGKHINHLL AKTFKAPAKE TKAASTEETT QQQPRQNDAA SHNNKQQPSG TSSRPASSAP
     SYRRESTSNN NNNAKRGSER DRSKRSDESV KAFTGRDRYG LNEGSSEEDK WRKKRVHKTK
     KQAEEHVVQC PAHIKIALPI TVKDLAAEMK LKASELIQKL FIHGMTYVVN DVLDSQTVVE
     YIGLEFGCTI EIDSSAKEKL CLVENTVRDE VNATDPEKLI IRSPIVAFMG HVDHGKTTII
     DALRQSNMAA SEAGAITQHT GAFKCTTPVG EITVLDTPGH EAFSAMRARG AEVCDIVVLV
     VAGDEGIKEQ TIEAIEHAKG ANITIVVAIN KCDKPNFNVE TVYRQLAELD LLPEAWGGSI
     ATINTSAKTG EGLQDLLEML ALQAEVLELK ADPSARARGL VIESELHKGL GAVATVLVQN
     GTLHLGEALV FNDCYGKVKT MHDEHNQLLQ SATPSTPVLI TGLSAIPKAG DPFIVVKNEK
     VAKEIISARL AGQQRSAALQ KKRPNFDAVL QNKKTLKLII KADVQGSIEA LAHSILNIRS
     EKVDVEILSS GVGDISESDI RLASASKATV IGFHTSVESH AEPLIKNLNV KVCLFDIIYH
     AVDAIKEIMT GLLDPIAEEK NLGAAEIKAT FKSSQLGTIY GCLVTEGTVV RNQKIRIIRD
     KEVLWKGSLS SLKRLKEDVK EVKKGMECGI LLDNYQQAQV GDILQCYEVI YHPQTL
 
 
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