IF2_CAUSK
ID IF2_CAUSK Reviewed; 1045 AA.
AC B0T167;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Caul_0033;
OS Caulobacter sp. (strain K31).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter; unclassified Caulobacter.
OX NCBI_TaxID=366602;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K31;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Stephens C., Richardson P.;
RT "Complete sequence of chromosome of Caulobacter sp. K31.";
RL Submitted (JAN-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; CP000927; ABZ69171.1; -; Genomic_DNA.
DR RefSeq; WP_012284129.1; NC_010338.1.
DR AlphaFoldDB; B0T167; -.
DR SMR; B0T167; -.
DR STRING; 366602.Caul_0033; -.
DR PRIDE; B0T167; -.
DR EnsemblBacteria; ABZ69171; ABZ69171; Caul_0033.
DR KEGG; cak:Caul_0033; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_3_5; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
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; IPR004161; EFTu-like_2.
DR InterPro; IPR013575; IF2_assoc_dom_bac.
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; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF08364; IF2_assoc; 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.
FT CHAIN 1..1045
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000075596"
FT DOMAIN 540..710
FT /note="tr-type G"
FT REGION 1..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..556
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 574..578
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 596..599
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 650..653
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 686..688
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 30..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..214
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 549..556
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 596..600
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 650..653
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1045 AA; 110522 MW; AB732A5B18AD7AF6 CRC64;
MSDENDNGRP GSNPGGRAPI TLKPRQGSVS AGVVKQSFSH GRTKTVVVET KRVRPHAPPA
GNLAAPSSAE RRQGDAPRQQ SSSGGGGSSA GGLSQGEMLA RQRAIEAARE HQERQAAERR
AAEARAASEA AAARDAAAKS AAAAKAAAAP APEAPAAPAP TPAPVAQAPA APVVQAPVVA
APVQAPAAPV AAAPAAPRAE APRPAPPPVR SDAPRPAPTA GQTRTYEPSR DRRDDRSSTT
TYRPGPGAPP QGDRPQGDRP QGDRPFNQRA PRPDGPYNQR TPRPDAGGPP RGPRPEGAGG
FRNDRPQGDR PQGDRPQGDR PQGDRPTQTV RYSALAPRPA PGARPGPGGP RGARPGVPAS
APATPEIQRA TRSAPRPGGD VGRKPEEDDD RRKAAAPGKA VSRAKGAPIR REGRLTIQTV
AGDGDSADRM RSLASVRRAR EREKEKRRGG PADVVKVARE VIIPDVITVQ ELSNRMAVRG
VEIIKFLMRQ GVMLKINDVI DNDTAELVAT EFGHTVRRVS EADVEEGFIG AEDVDDHLEP
RPPVVTVMGH VDHGKTSLLD ALRKADVASG EHGGITQHIG AYQVRLESGQ KVTFLDTPGH
AAFSQMRARG ANITDLVILV VAGDDGVMPQ TVEAIKHARA AEVPIIVAVN KMDKPGADST
RVVNELLQHE IVVESLGGDT QIVEVSAKTG QGLDELIERI LLLAEVMDLK ANPDRTADGV
VIEAKLDKGR GAVSTVLVKR GTLKRGDIVV AGSQFGRVRA LLNERNEQLT EAGPATPVEI
LGLDGVPSPG DPFAVVENEA RARELTEYRI RLKREKSMHP VGAGATSMAD MMAKLQDKKY
RELPLVIKAD VQGSAEAIIG SLDAMSTDEV RARIILSGAG AISESDVMLA KGAGAPLIGF
NVRASAQARA LAEREGVEIR YYAIIYDLLD DIKGVLSGML APIQRETFLG NAEVLQAFDI
SKVGKVAGCR VTEGVVRKGA KVRIIRNDIV VLELGTLQTL KRFKDEVPEV PSGQECGMMF
AGFQDIKVGD TIECFTVEEI KRQLD
