IF2_CHLT2
ID IF2_CHLT2 Reviewed; 896 AA.
AC B0B9K4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CTL0351;
OS Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=471472;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=434/Bu / ATCC VR-902B;
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; AM884176; CAP03791.1; -; Genomic_DNA.
DR RefSeq; WP_009873552.1; NC_010287.1.
DR RefSeq; YP_001654435.1; NC_010287.1.
DR AlphaFoldDB; B0B9K4; -.
DR SMR; B0B9K4; -.
DR EnsemblBacteria; CAP03791; CAP03791; CTL0351.
DR KEGG; ctb:CTL0351; -.
DR PATRIC; fig|471472.4.peg.379; -.
DR HOGENOM; CLU_006301_3_1_0; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000000795; 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_1000093770"
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
