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Database: UniProt
Entry: IF2_CHLTE
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Original site: IF2_CHLTE 
ID   IF2_CHLTE               Reviewed;         914 AA.
AC   Q8KFT1;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 126.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CT0241;
OS   Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS   (Chlorobium tepidum).
OC   Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC   Chlorobaculum.
OX   NCBI_TaxID=194439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX   PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA   DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA   Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA   Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA   Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA   White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA   Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT   anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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; AE006470; AAM71487.1; -; Genomic_DNA.
DR   RefSeq; NP_661145.1; NC_002932.3.
DR   RefSeq; WP_010931933.1; NC_002932.3.
DR   AlphaFoldDB; Q8KFT1; -.
DR   SMR; Q8KFT1; -.
DR   STRING; 194439.CT0241; -.
DR   EnsemblBacteria; AAM71487; AAM71487; CT0241.
DR   KEGG; cte:CT0241; -.
DR   PATRIC; fig|194439.7.peg.233; -.
DR   eggNOG; COG0532; Bacteria.
DR   eggNOG; COG3170; Bacteria.
DR   HOGENOM; CLU_006301_0_1_10; -.
DR   OrthoDB; 9811804at2; -.
DR   Proteomes; UP000001007; 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; cd01887; IF2_eIF5B; 1.
DR   CDD; cd03702; IF2_mtIF2_II; 1.
DR   CDD; cd03692; mtIF2_IVc; 1.
DR   Gene3D; 1.10.10.2480; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR   HAMAP; MF_00100_B; IF_2_B; 1.
DR   InterPro; IPR004161; EFTu-like_2.
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   NCBIfam; TIGR00487; IF-2; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF11987; IF-2; 1.
DR   Pfam; PF04760; IF2_N; 1.
DR   SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 2.
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; Reference proteome.
FT   CHAIN           1..914
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000137190"
FT   DOMAIN          411..581
FT                   /note="tr-type G"
FT   REGION          246..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          293..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          420..427
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          445..449
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          467..470
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          521..524
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          557..559
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        246..267
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         420..427
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         467..471
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         521..524
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   914 AA;  100647 MW;  7FAC8C39E666EF1E CRC64;
     MAIEEKQSRF RISDIAKELQ VSPREVLQFV KQAGGKVAST SSMVGEDMRD MIFGNFSQEK
     KRVDEARKIR AEKQKRLTRL EEQSRKAYEK EQQLKESLSI APLPAPVLHA PEVKIEIPPE
     TATTPVAAEP PAILPVVSTP QPEPVADLPL VTEPVVAEPV AEAEPVVEAP VAETAGPEVM
     TPLVQTLPES MQAYEAPQKI GGLTVLGTID VISEAERKKK SRKKSFRESA VELKGEFENV
     LSVDSEDGEA AKKKAAKPDG GEDVGVKKKK GKKKKKVEID DKVISKNIKS TISGMDDSGL
     SGSRQKFRKQ RRMEREREFE EAEAMREAEK TLIRVTEYAS PHELAELMGL TAKEIIQKCF
     SMGKFVTINQ RLDKETIELI GLEFGFEVEF ISEIEATTTE ELVDNAEDLQ TRPPVVTIMG
     HVDHGKTSLL DYIRRSNVVA GESGGITQHI GAYEVSLDDG RHITFLDTPG HEAFTAMRAR
     GAQVTDIVIL VVAADDSVMP QTIEAINHAK AAGVPIVVAI NKIDKPEANV EKIKAQLSEA
     GVLVEDWGGE SQCQEISAKK GIGISELLEK VLAEAEIREL KGNYSRDILA SGVIVESELD
     KGKGVVSTVL VQRGFLKVGD PFVAGNSMGK VRALMDERGK RIHEAGPSTP VRVLGFEDMP
     QSGDVLTVMA SDRDARDLAQ KRQIIKREHE FRRSTRVKLD SIARQIKEGL KKELSVIIKA
     DTDGSIQALA DGLMKIHNEE VKVQIIHQGV GQITETDVLL AAASDAIIIG FRVRPNVNAK
     RLAEKEDLDV RFYSVIYHVL EDVEKALEGM LSPELHEESL GSLEIRQVFR VPKVGNVGGA
     YVLEGKVSRD AKVRLLRDGV QIFEGQLDSL KRFKDDVKEV DAGYECGVSL KGYDDIKVGD
     VIEAYKIVEK KRKL
//
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