IF2_CHLCH
ID IF2_CHLCH Reviewed; 1022 AA.
AC Q3AQK7;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Cag_1462;
OS Chlorobium chlorochromatii (strain CaD3).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=340177;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CaD3;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Chlorobium chlorochromatii CaD3.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000108; ABB28718.1; -; Genomic_DNA.
DR RefSeq; WP_011362482.1; NC_007514.1.
DR AlphaFoldDB; Q3AQK7; -.
DR SMR; Q3AQK7; -.
DR STRING; 340177.Cag_1462; -.
DR EnsemblBacteria; ABB28718; ABB28718; Cag_1462.
DR KEGG; cch:Cag_1462; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_0_1_10; -.
DR OMA; KPGANTE; -.
DR OrthoDB; 79988at2; -.
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; 2.
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..1022
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228184"
FT DOMAIN 519..689
FT /note="tr-type G"
FT REGION 82..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..535
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 553..557
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 575..578
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 629..632
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 665..667
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 394..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 528..535
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 575..579
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 629..632
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1022 AA; 111719 MW; 7300B11E6D0EE9A7 CRC64;
MTLGESEKRY RISDIARELQ LSPQEVLQFV KQQGVKVAST SSMVNEEVHG LIINQFSAEK
KMVDETLKIR AEKEKRLTRL EEQSRKTLEK EQHLMEAISP TVRASKSSAK GSESAPKSEP
KKSKQAVPAA AMVDDVPAAV VQQVVAEPEV VEPTPVVEVE APALEPAIIS EHVVDAEPIE
NAVTVAPVEV VVNEPIETVE SVEPEFVVAE VTPLEPIAQS TIEIVAEGES VEVAEALHVA
EPVVAIPPIT ETAELSDSTV EPIEPIASVP STAPAPPARR EPTVNENLVS FAAPQMMGGL
TVVGTLDMHT GRGRKNRKKN FREQADALKG EFEVKAAAPV ASENKTEAGV AKKSKPAAEV
KPKPATTTAA DDAKKAKKGK KKKKPDVDEK VISANIQKTI SGIDDRSGTG SRQKFRKMRR
SEREREQEEG AAQRELEQSI VRVTEFASPH ELAELMGITA KDIIQKCFGL GKFVTINQRL
DRESIELIAL EFGFEAEFIS EVEATAVETE ADAEEDLQTR PPVVTIMGHV DHGKTSLLDY
IRKSRVVAGE SGGITQHIGA YEVTVDGDRK ITFLDTPGHE AFTAMRARGA QVTDIVILVV
AADDNVMPQT IEAINHAKAA GVPIVVALNK IDKSEANPDK IKTQLSEAGV LIEEWGGVYQ
CQEISAKKGI GIVELMEKVL TEAELRELKG NYSREVLASG VIVESELDKG KGVVSTVLVQ
RGVLKVGDPF VAGNSLGKVR ALMDERGKRI LLAFPSQPVR VLGFEDLPQS GDVLTVMASE
RDARDLAQKR QIIRREHDFR RSTRVKLDSI ARQIREGVMK ELNVIIKADT DGSIQALADG
LMKIQNDEVK VQLIHQGVGQ ITETDVLLAA ASDAIIIGFR VRPNVNAKKL AEKEDLDIRF
YSVIYHVLED VETALEGMLS PELHEESLGS IEIRQIFRVP KVGNVGGCYV LEGKVPRDAK
VRLLRDGVQI YEGQLAALKR FKDDVKEVDS GYECGLSLKN YDDIKVGDVV EAYRIVEKKR
KL
