IF2_CHLL2
ID IF2_CHLL2 Reviewed; 952 AA.
AC B3EFB1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Clim_0300;
OS Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290315;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 245 / NBRC 103803 / 6330;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Zhao F., Li T., Liu Z.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium limicola DSM 245.";
RL Submitted (MAY-2008) 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; CP001097; ACD89394.1; -; Genomic_DNA.
DR RefSeq; WP_012465275.1; NC_010803.1.
DR AlphaFoldDB; B3EFB1; -.
DR SMR; B3EFB1; -.
DR STRING; 290315.Clim_0300; -.
DR EnsemblBacteria; ACD89394; ACD89394; Clim_0300.
DR KEGG; cli:Clim_0300; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_0_1_10; -.
DR OMA; KPGANTE; -.
DR OrthoDB; 79988at2; -.
DR Proteomes; UP000008841; 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; 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; Reference proteome.
FT CHAIN 1..952
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000190629"
FT DOMAIN 449..619
FT /note="tr-type G"
FT REGION 74..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..465
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 483..487
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 505..508
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 559..562
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 595..597
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 153..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 458..465
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 505..509
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 559..562
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 952 AA; 105920 MW; 130376E57AB803B4 CRC64;
MAIEEMEKKY RISDIARELQ VSPQEVLQFV KLEGGKVAST SSMVDQGMRE LIFGHFSNEK
KMVDETMKIR QEKQRRLSRL EEQSRKTYEK ERQLKETLHS ASVAPAVHEE KKEPVVPEVR
LVVSVPDELV SSEKVEEIEQ IEQPVQLEQP VMAAQADQTD QTDQTDQADQ ADRTDQVIQT
DQPVQEEPLE EVPAPKEMPV KEEPSVNEQL VSFETPKNIG GLTVIGTLDM HSPFDRSSEA
ERKKKNRKKN FKEQADALKS EFDTTVKEEV AADEKGAVKK KPAKPPGETN AATPAGTAST
AGAQPLKKGK KKKKPDVNDK VISANIRTTI SGMDDSGGTG SRQKFRKLRK IERERESEAA
EAFRESQQMI VRVTEYASPH ELADLMGVTA KDIIQKCFSL GKFVTINQRL DKESIELIAL
EFGFEAEFIS EVEATAVLIE ADEPEDMQIR PPVITIMGHV DHGKTSLLDY IRNSNVVAGE
SGGITQHIGA YEVTVESDRK ITFLDTPGHE AFTAMRARGA QVTDIVILVV AADDSVMPQT
IEAINHAKAA GVPIVVAINK VDKPEANPEK IKTQLSEAGV LVEEWGGEYQ CQEISAKKGI
GIAELMEKVL AEAEIRELKG NFSREINANG IIVESELDKG KGVISTVLVQ RGFLKIGDPF
VAGNTMGKIR ALMDERGKRI LFAGPSQPVR VLGFEELPQS GDVLTVMSSD RDARDLAQKR
QVIRREHEFR RSTRVKLDSI ARQIKEGLMK ELSMIIKADT DGSIQALADG LMKIQNEEVK
VQIIHQGVGQ ITETDVLLAA ASDAIIIGFR VRPNVNAKKL AEKEDLDVRF YSVIYHVLED
VEKALEGMLS PELHEESLGS LEVRQVFRVP KVGNVGGCYM LEGKVFRDSK VRLLREGVQI
YDGQLDALRR FKDDVKEVDA GYECGISLKN YDDIKVGDIV EAYRIVEKKR KL
