IF2_GEOSL
ID IF2_GEOSL Reviewed; 883 AA.
AC Q74CT3;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=GSU1588;
OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=243231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX PubMed=14671304; DOI=10.1126/science.1088727;
RA Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA Lovley D.R., Fraser C.M.;
RT "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT environments.";
RL Science 302:1967-1969(2003).
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; AE017180; AAR34962.1; -; Genomic_DNA.
DR RefSeq; NP_952639.1; NC_002939.5.
DR RefSeq; WP_010942233.1; NC_002939.5.
DR AlphaFoldDB; Q74CT3; -.
DR SMR; Q74CT3; -.
DR STRING; 243231.GSU1588; -.
DR EnsemblBacteria; AAR34962; AAR34962; GSU1588.
DR KEGG; gsu:GSU1588; -.
DR PATRIC; fig|243231.5.peg.1629; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_7; -.
DR InParanoid; Q74CT3; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000000577; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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..883
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228201"
FT DOMAIN 383..552
FT /note="tr-type G"
FT REGION 118..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..399
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 417..421
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 438..441
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 492..495
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 528..530
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 186..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 392..399
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 438..442
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 492..495
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 883 AA; 95693 MW; 5AFCBFDA7EA7640B CRC64;
MSKTHVYELA KKMGIENKEL LTRLKSLGIE VKNHLSVLEE DEILKVTAPP AAPPKSGPQE
EVRVTTTVIR RRRVAEAAPA ETPVEAVAPP VESAPAPLEV EAVEEAVVQA PPVVEPPVAR
ESEAAPAEEP VAAAVKPASE PPVVQKAPVA PAAPPVDDKP TANKARILGR VELPGITTPA
PKPADRREAT APKKRIEERI MTPSPTDRPA PAGDDRRKAG TPPPPPRKGK EFVAPAEPER
GAKKPGGGGA GKKKEAFKKT ELLEKRERIF EPGPKTGKGK KRERDMVSLG RKTEITVPKA
IKRIIKISES ITVGELAKRM GVKATDLIRV LMKMGMMVTI NHPLDVDTAT LVASEFGYEI
ENVAIDVDEM LESVPDAPES LTKRPPVVTI MGHVDHGKTS LLDAIREANV IAGEAGGITQ
HIGAYDVELN GRKITFLDTP GHEAFTAMRA RGAKVTDIVI LVVAADDGVM PQTREAVNHS
KAAGVPIIVA INKIDKPEAK PERVKQELME FGLVSEEWGG ETIFVEVSAK KRINLPELLE
MVLLQADVMD LKANPDKDAR GTIVEAKLDR GRGPVATVLV QEGTLKIGDY FVAGVNSGRV
RAMQNDRGDK VNEAGPSMPV EVIGFTGVPD AGDVFISLVD EKRAKEIASH RQQKLRETEL
AKHSKMSLEQ LYDKIQKGEV KDLNAIVKAD VQGSVEAVSE SLRKLSTDAV RLNVIHSSVG
AITETDVNLA SASNAIILGF NVRPEPKASA HAEKEGVDIR LYNIIYDAVE DIKKAMEGLL
EPTLREKYLG RAEVREVFSV PKVGNVAGCY IQDGKMIRNA QVRLLRDNVV IYEGKMSSLR
RFKDDVKEVA TGYECGIGLE NYNDIKVGDV IEDFEIEKIA TTL
