IF2_CHLMU
ID IF2_CHLMU Reviewed; 896 AA.
AC Q9PKU0;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Translation initiation factor IF-2;
GN Name=infB; OrderedLocusNames=TC_0371;
OS Chlamydia muridarum (strain MoPn / Nigg).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=243161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MoPn / Nigg;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AE002160; AAF39229.1; -; Genomic_DNA.
DR PIR; G81709; G81709.
DR RefSeq; WP_010230269.1; NZ_CP027217.1.
DR AlphaFoldDB; Q9PKU0; -.
DR SMR; Q9PKU0; -.
DR STRING; 243161.TC_0371; -.
DR PRIDE; Q9PKU0; -.
DR EnsemblBacteria; AAF39229; AAF39229; TC_0371.
DR GeneID; 1245723; -.
DR KEGG; cmu:TC_0371; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_3_1_0; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000800; 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.
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_0000137188"
FT DOMAIN 401..570
FT /note="tr-type G"
FT REGION 32..306
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..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..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:0000250"
FT BINDING 456..460
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 510..513
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 896 AA; 97498 MW; FD9D4FE9D06A677B CRC64;
MEHAKLTKNL KLKIKNAQLT KAAGLDKLKQ KLAQAGSSDT KNSPVSKAQT KEKSSKKTAG
TTASAPEIES GATESTARRI RAKDRSSFAA EEPSTTVALP GDASHLTLDA LPSADSTEPL
SNSSQEKIVE DAVETPNSPQ EDGKELQEEV ANEQPARNEE TPIIRTRTEP KSVVSIKPKF
GPTGKHINHL LAKTFKAPAK ETKAAAPAEE TTQQTRPSVE TASTKQQQPS GTNTRPAQSA
PAYRRESTNN NNNSKRGPDR DRTKRSDENV KAFTGRDRYG LNEGSSEEDK WRKKRVHKTK
KQSEEHVVQC PSHIKIALPI TVKDLAAEMK LKASELIQKL FIHGMTYVVN DVLDSQTVVQ
YIGLEFGCTI EIDSSEKEKL CLVENTVRDE INETNPQKLV IRSPIVAFMG HVDHGKTTLI
DALRQSNMAA SEAGAITQHM GAFKCSTPVG EITVLDTPGH EAFSAMRARG AEVCDIVVLV
VAGDEGIKEQ TVEAIEHAKA ANITIVVAIN KCDKPNFNEE TVYRQLAELN LLPEAWGGSI
ATINTSAKTG EGLQDLLEML ALQAEVLELK ADPSARARGL VIESELHKGL GAVATVLVQN
GTLHLGEALV FNDCYGKIKT MHNEHNQLLQ SASPSTPVLI TGLSAIPKAG DPFIVVKNEK
VAKEIISARL AGQQRSAALQ KKRPNFDAVL QNKKTLKLII KADVQGSIEA LAHSILNIRS
EKVDVEILSS GVGDISESDI RLASASKATV IGFHTSVESH AESLIKSLNV KVCLFDIIYH
AVDAIKEIMT GLLDPIAEEK NLGAAEIKAT FKSSQLGTIY GCLVTEGTMV RNQKVRIIRD
KEVLWKCSLS SLKRLKEDVK EVKKGMECGI LLDNYQQAQI GDTLQCYEVI YHPQKL
