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 03-AUG-2022, entry version 120.
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; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; 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 OMA; NRDNRTG; -.
DR OrthoDB; 79988at2; -.
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; 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; 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
