IF2_ERYLH
ID IF2_ERYLH Reviewed; 832 AA.
AC Q2NC10;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=ELI_03445;
OS Erythrobacter litoralis (strain HTCC2594).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=314225;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2594;
RX PubMed=19168610; DOI=10.1128/jb.00026-09;
RA Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.;
RT "Complete genome sequence of Erythrobacter litoralis HTCC2594.";
RL J. Bacteriol. 191:2419-2420(2009).
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; CP000157; ABC62781.1; -; Genomic_DNA.
DR RefSeq; WP_011413657.1; NC_007722.1.
DR AlphaFoldDB; Q2NC10; -.
DR SMR; Q2NC10; -.
DR STRING; 314225.ELI_03445; -.
DR EnsemblBacteria; ABC62781; ABC62781; ELI_03445.
DR KEGG; eli:ELI_03445; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_1_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000008808; 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; 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; 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.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..832
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008242"
FT DOMAIN 333..503
FT /note="tr-type G"
FT REGION 1..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..349
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 367..371
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 389..392
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 443..446
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 479..481
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..84
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 342..349
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 389..393
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 443..446
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 832 AA; 90667 MW; EA2847DA65BB7983 CRC64;
MSDDNDKPRT RKPLGLKRSV DAGEVKQTFS HGRTNKVAVE VKRKRKLLKP GETPAPAPEP
APEPAPAPAP APAAKKPAPK KPAPAAETPQ ERVARLQREA EEERLKLAED ARKRDDQKAK
QNADDEKKRQ EENKKAEEEA EKQAAAEAEA AAAAEAAPEE DADDGRKAPV ARKFTPVARP
EPKRPEKKKE EKKPARGGAK DKRRSGKLTV SKALNEDEGR RAMSLAKLKR AREKERRLKG
GGSSAPREKQ VRDVIVPEAI TVGELAKRMG EKGADLVKEL FNLDMMVTVN QTIDQDTAEL
LVEQFGHNIQ KVSEADVDIQ AEEDVDPEET LQPRPPVVTI MGHVDHGKTS LLDALRGTNV
TKGEAGGITQ HIGSYQVNTK SGGKVTFLDT PGHAAFSEMR QRGANVTDIV VLVVAADDGV
MPQTIEAIKH TKAAGVPMIV AINKCDKPEA DPDNIRNRLL EHEIIVEKLS GDVQDVEISA
TKKTGLDELL EKIELQAELL ELKARPDRMA EATVIEAQLD KGRGPVATVL ITRGTLKRGD
TFVVGTESGR VRAVVNDQGK QIKEAGPSMP VEVLGLGGVP GAGDQLTVVE NEQRAREVAE
YRQEKATEKR TALAPTSFDT MFNNLQSNVI EWPVLVKADV QGSVEAIVTA LHNISNDEIK
VRVLHAGVGA ITESDVTLAA ASNAPIIGFN VRPNAKAREL VKRDDVRMMY YDVIYHLTDE
VAKEMAGELG PERIETVVGR ADVKEVFKSG KKDKAAGLLV TDGVIRKGLF ARLTRDDVIV
SATTIASLRR FKDDVDEVRS GLECGVVLED TNDIQPGDSL EVFEVEERER TL
