IF2_FRAP2
ID IF2_FRAP2 Reviewed; 844 AA.
AC B0TWR3;
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=Fphi_0948;
OS Francisella philomiragia subsp. philomiragia (strain ATCC 25017 / FSC 153 /
OS O#319-036).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=484022;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25017 / FSC 153 / O#319-036;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Richardson P.;
RT "Complete sequence of chromosome of Francisella philomiragia subsp.
RT philomiragia ATCC 25017.";
RL Submitted (DEC-2007) 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; CP000937; ABZ87171.1; -; Genomic_DNA.
DR RefSeq; WP_012280356.1; NC_010336.1.
DR AlphaFoldDB; B0TWR3; -.
DR SMR; B0TWR3; -.
DR STRING; 484022.Fphi_0948; -.
DR PRIDE; B0TWR3; -.
DR EnsemblBacteria; ABZ87171; ABZ87171; Fphi_0948.
DR KEGG; fph:Fphi_0948; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_1_6; -.
DR OMA; NRDNRTG; -.
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; 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; 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.
FT CHAIN 1..844
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000075606"
FT DOMAIN 343..510
FT /note="tr-type G"
FT REGION 120..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..359
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 377..381
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 398..401
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 452..455
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 488..490
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 156..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 352..359
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 398..402
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 452..455
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 844 AA; 91762 MW; EBA7F17A12CBA798 CRC64;
MAEITVGQLA QQTNKEVSTL LKQLKSFGIE KSSEKDTLTP EEMKTLLDKI NSAKNTVTRK
KVTSLKLDGK HKINVSVKKK RRVAKKVEEQ SPAKVEESIV EKPQAAVDVK DNKAVESVER
NSVNLVQPQQ EKPVTKPVIK DNGFKITAMP EVKIQENNSQ DEEKSSEDKS TESKNNKKKS
PKKVFTESGN NTNTKYKREE EEKKSKAKKA SGKGFKKANP RQLSQLAGDL ESFDEFGSKK
GKLKAPKVKK QEFTMPVESA VKTIEIREGI TVSDLANRMA VKGAEIVKVL FNMGVMATIN
QSLDQDTAVL IVEEMGHKYT LHNENALEEA VTTVDRSLHK KISRAPVVTI MGHVDHGKTS
LLDYIRKARV VAGEAGGITQ HIGAYSVKTS KGAITFLDTP GHEAFTSMRA RGAKSTDIVI
LVVAADDGVM PQTEEAIQHA KAAGVPIVVA VNKIDKPDAD PDKVVGELAQ RNVIPESWGG
DVMFANVSAK TGEGVAELLD AVLLQSEVLE LEAFAEGLAE GVVIESRLEK GRGPVATVLV
QNGSLKQGDN ILCGTEYGRV RAMHDDLGKQ IKVAGPATPV EILGLSGVPA AGDDMVVIEN
EKKAKELAAQ RSQRQKEAKI AQEQSLKLSN MFSNMGKEGE QQTLKIILKG DVQGSVEAIR
ESLLKLSTDE VKVDIIASGI GAITSSDVTL AVASTAVIIG FNVRADSAAK KLAEVDGVEL
RYYNIIYDLI DDVKKAMTGL LSPDMKEQII GIAEVREVYR SSKFGSIAGC MVVEGAVKRT
NPIRVLRDNV VIYEGTLESL KRFKDDASEV KKGMECGIGV KNYNDVREGD QIEVFEVIEV
AKEL
