IF2_CHLPD
ID IF2_CHLPD Reviewed; 991 AA.
AC A1BDF1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN OrderedLocusNames=Cpha266_0369;
OS Chlorobium phaeobacteroides (strain DSM 266).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290317;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 266;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.,
RA Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium phaeobacteroides DSM 266.";
RL Submitted (DEC-2006) 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; CP000492; ABL64428.1; -; Genomic_DNA.
DR RefSeq; WP_011744261.1; NC_008639.1.
DR AlphaFoldDB; A1BDF1; -.
DR SMR; A1BDF1; -.
DR STRING; 290317.Cpha266_0369; -.
DR PRIDE; A1BDF1; -.
DR EnsemblBacteria; ABL64428; ABL64428; Cpha266_0369.
DR KEGG; cph:Cpha266_0369; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_0_1_10; -.
DR OMA; KPGANTE; -.
DR OrthoDB; 79988at2; -.
DR Proteomes; UP000008701; 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..991
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008225"
FT DOMAIN 488..658
FT /note="tr-type G"
FT REGION 126..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..504
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 522..526
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 544..547
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 598..601
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 634..636
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 131..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 497..504
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 544..548
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 598..601
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 991 AA; 109017 MW; 233D8F221A5EC5CB CRC64;
MALEDMEKRY RISDLSRELQ VSPQEVLQFI RMNGGKVGST SSMVNEEMRG MIFGNFSVEK
KMVDEAMKIR AEKQRRLTRL EEQSRKTYEK EQQLRDSMHV APLVPVAPLH VAQDVIVEVA
APPSAQADHT VQAEPAVQTE SAVQTESAVQ TESAVQTEPA VQTEPAVQTE PEVQTEPAAQ
TEPEVQTEPA AQTEPAAQTE PAAQTESAVQ TEADLSDVGE VSIVPENVEV IDVPELPMVP
VMPVKEEPSV NDQLVSFDIP QNIGGLTVVG TLDMMNPFDR SESGKMKARK KNFKEQADAL
KSEFDTPAGE EKLVDDKLVV KKKPVKAAGD GDTAPAADDA LAGKKKPGKK KKKPDVDEKV
ISANIRTTIS GMDDSAGSVS RQKFRKMRRM EREKEHEAAE AFRESQRAIV RVTEYASPHE
LAELMGVTAK EIIQKCFALG KFVTINQRLD KESLELIALE FGFEAEFISE IEATAVVAEV
DDAEDLLIRP PVVTIMGHVD HGKTSLLDYI RNSNVVAGES GGITQHIGAY EVTVEGNRKI
TFLDTPGHEA FTAMRARGAQ VTDIVILVVA ADDSVMPQTI EAINHAKAAG VPIVVAINKI
DKPAANPEKI KTQLSEAGVL VEDWGGEYQC QEISAKQGIG IEELMGKLLT EAEIRELKGN
FSEDVLASGI IIESELDKGK GVISTVLVQR GYLRVGDPFV AGNTMGRVRA LMDERSKRIH
EAGPSQPVRV LGFEALPQSG DVLTVMASDR DARELAQKRQ VIRREHEFRR STRVKLDSIA
RQIREGLMKE LSVIIKADTD GSIQALADGL MKIHNEEVKV QIIHQGVGQI TETDVLLAAA
SDAIIIGFRV RPNVNAKKLA EKEDLDVRFY SVIYHVLEDV EKALEGMLSP ELHEESLGSL
EIRQVFRVPK VGNVGGCYAL EGKVFRDSKV RLLRDGVQVY DGQLDTLRRF KDDVKEVDAG
YECGLSLKNY DDIKVGDIVE AYKIVEKKRK L
