IF2_CELJU
ID IF2_CELJU Reviewed; 930 AA.
AC B3PI96;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CJA_0436;
OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS cellulosa).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=498211;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ueda107;
RX PubMed=18556790; DOI=10.1128/jb.01701-07;
RA DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA Nelson K.E.;
RT "Insights into plant cell wall degradation from the genome sequence of the
RT soil bacterium Cellvibrio japonicus.";
RL J. Bacteriol. 190:5455-5463(2008).
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; CP000934; ACE84775.1; -; Genomic_DNA.
DR RefSeq; WP_012486117.1; NC_010995.1.
DR AlphaFoldDB; B3PI96; -.
DR SMR; B3PI96; -.
DR STRING; 498211.CJA_0436; -.
DR PRIDE; B3PI96; -.
DR EnsemblBacteria; ACE84775; ACE84775; CJA_0436.
DR KEGG; cja:CJA_0436; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_0_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001036; 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; IPR009061; DNA-bd_dom_put_sf.
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; 2.
DR SUPFAM; SSF46955; SSF46955; 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..930
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093767"
FT DOMAIN 431..600
FT /note="tr-type G"
FT REGION 160..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..447
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 465..469
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 486..489
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 540..543
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 576..578
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 208..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 440..447
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 486..490
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 540..543
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 930 AA; 100715 MW; E4DE42CEAB5E9694 CRC64;
MAEVTVNELA TSIGAPVERL LKQMQEAGLQ HKTASAKVSD EEKQRLLAYL KGSHGEAAVE
PRKITLQRKT TTTIKTGTGN AKKTVNVEVR KKRTYVKRED DVVDNTQAAQ SQEQDDELAS
TVVEEVQQAE PSVVPVVDVA PEPEPEPVVE EVDVAAEEAE PVEAAVDTSA PTRFSFTDGI
EEKRRAAIER RQAEEAARQA ELKAIEEAKR AAEEAKRTQP RAEKPADKSA AAGKGAKPDN
RQPAKGKQAP VAVPVEREDA KHGHGHKKHH HGRNDDDFDD DSADRGNKRG AGKAVKKAAA
PKKSSKIDLL DFVGDDSEDS DVLARRSHIR AHHKKNNKHA FKKPTTQIVH EIDIPETIAV
SELAQRLTIK VGELIKRLMK MGVMASMNEQ IDQDTAVLIV EELGHKANLV SENDIEHALE
KSLETAGELT TRAPVVTVMG HVDHGKTSLL DYIREAKVAA GEAGGITQHI GAYRVTTSRG
EITFLDTPGH AAFTAMRARG AKATDVVILV VAADDGVMPQ TEEAIMHARA AEVPIVVAIN
KCDKPSADPD RVTNELVAKG VIPEAYGGDT QFVQVSAHTG QGIDELLEAI SLQAEVLELT
AVTNAAAKGV VIEARVDKGR GTVATVLVQQ GTLKQGDLIL AGQSYGRVRA MVNERGEQVK
EAGPSTPVEI LGLDMPPSAG DDFVVLDDER KAREVAAFRA EKERKEKLAR FQAAKLENMF
SNMEAGQKKT LTVVIKADVR GSLEAIQASL ADIGNDEVQV NVISSGIGGI TENDVNLAVT
SGAIIVGFNV RADGATRRLA ETEGVDIRYY SIIYQLLDEV KAALSGMLDP ERVETIVGIA
NVREVFNSPK FGQVAGCMVV EGTVYRNKPI RVLRDNVVIF TGELESLRRF KDDVNEVRNG
FECGIGVKNY DVKVGDQIEV YEVKEVARQL
