IF2_RUEPO
ID IF2_RUEPO Reviewed; 835 AA.
AC Q5LWL4;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SPO0061;
OS Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS pomeroyi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=246200;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX PubMed=15602564; DOI=10.1038/nature03170;
RA Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT environment.";
RL Nature 432:910-913(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA Rivers A.R., Smith C.B., Moran M.A.;
RT "An updated genome annotation for the model marine bacterium Ruegeria
RT pomeroyi DSS-3.";
RL Stand. Genomic Sci. 9:11-11(2014).
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; CP000031; AAV93392.1; -; Genomic_DNA.
DR RefSeq; WP_011045834.1; NC_003911.12.
DR AlphaFoldDB; Q5LWL4; -.
DR SMR; Q5LWL4; -.
DR STRING; 246200.SPO0061; -.
DR EnsemblBacteria; AAV93392; AAV93392; SPO0061.
DR KEGG; sil:SPO0061; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_1_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001023; 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.
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..835
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228244"
FT DOMAIN 332..500
FT /note="tr-type G"
FT REGION 1..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..348
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 366..370
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 388..391
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 442..445
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 478..480
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 16..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 341..348
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 388..392
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 442..445
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 835 AA; 90200 MW; 543CC094F33DD84A CRC64;
MSDTDGKKTL GLRGSRPGNV KQSFSHGRTK NVVVETKRKR VVVPKPGAGK PSAGGSSPAG
DPSRRPAGIS DAEMERRLNA LKAAKARESE EAAQREAEEK ARAEERERRR AEQEAKEREQ
REAEQRAREK AEEEERQRRE AEEEAKRAAV RAAAEQEAPK AERSAERAPA AARPEGGDNA
RRTTDRDRER EQRQTRGKGR QDGRRSGKLT LSQVTDGEGG RQKSLAAMKR KQERARQKAM
GGAAEREKVI REVQLPEAIV VSELANRMAE RVADVVKELM KMGMMVTQNQ TIDADTAELI
IEEFGHKVVR VSDSDVEDVI SDIEDAEEDL KPRPPVITIM GHVDHGKTSL LDAIRDAKVV
AGEAGGITQH IGAYQVKTDG GATLSFLDTP GHAAFTSMRS RGAQVTDIVV LVVAADDAVM
PQTVEAINHA KAAGVPMIVA INKIDKPEAN PTKVRTDLLQ HEVVVEAMSG EVQDVEVSAK
TGEGLDELLE AIALQAEILE LKANPDRPAQ GAVIEAQLDV GRGPVATVLI QKGTLRQGDI
FVVGEQYGKV RALINDKGER VSEAGPSVPV EVLGLNGTPE AGDVLNVTST EAQAREIAEY
RAQVAKDKRA AAGAATTLEQ LMAKAKADEN VAELPILVKA DVQGSAEAIV QAMEKIGNDE
VRVRVLHSGV GAITETDVGL AEASGAPIMG FNVRANASAR NTANQKGVEI RYYSVIYDLV
DDVKAAASGL LSAEIRENFI GYANIKEVFK VSNVGKVAGC LVTEGVARRS AGVRLLRDNV
VIHEGTLKTL KRFKDEVAEV QSGQECGMAF ENYDDIRPGD VIEIFEREEV TRTLT
