IF2_LISMF
ID IF2_LISMF Reviewed; 782 AA.
AC Q71ZZ7;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN OrderedLocusNames=LMOf2365_1342;
OS Listeria monocytogenes serotype 4b (strain F2365).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=265669;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F2365;
RX PubMed=15115801; DOI=10.1093/nar/gkh562;
RA Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA Luchansky J.B., Fraser C.M.;
RT "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT pathogen Listeria monocytogenes reveal new insights into the core genome
RT components of this species.";
RL Nucleic Acids Res. 32:2386-2395(2004).
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; AE017262; AAT04117.1; -; Genomic_DNA.
DR RefSeq; WP_003727494.1; NC_002973.6.
DR AlphaFoldDB; Q71ZZ7; -.
DR SMR; Q71ZZ7; -.
DR KEGG; lmf:LMOf2365_1342; -.
DR HOGENOM; CLU_006301_5_1_9; -.
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; 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.
FT CHAIN 1..782
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137218"
FT DOMAIN 283..452
FT /note="tr-type G"
FT REGION 47..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..299
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 317..321
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 338..341
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 392..395
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 428..430
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 64..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 292..299
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 338..342
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 392..395
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 782 AA; 84955 MW; C0B318A5DDA12F77 CRC64;
MSKVRVYEYA KEHQVSSKKV IEALKDLGIE VANHMSTINE NALRQLDNAI DGTNKKAEAP
KKETTSNENG NSKGPNKPNM TNSNEKSNKP NNPAGQANKP ATANKSQGAK PATNKPANTS
KQTQSSGNQQ QAGGQKRNNN NNSNRPGGGN PNRPGGNNRP NRGGNFNNKG RNTKKKGKLN
HSTVPPTPPK PKELPEKIVF SESLTVAELA KKLYREPSEL IKKLFMLGVV ATINQSLDKD
AIELICDDYG VQVEEEIKVD VTDLDVYFEN ELNEAVDESK LVERPPVVTI MGHVDHGKTT
LLDSLRNTKV TLGEAGGITQ HIGAYQLEIH DKKITFLDTP GHAAFTAMRA RGAQITDITI
LVVAADDGVM PQTIEAINHA KAAGMPIIVA VNKIDKPQAN PDRVMQELTE YELVPEAWGG
DTIFAPISAK FGEGLENLLD MILLVSEVEE LKANPDRRAI GSVIEAELDK GRGPVATLLV
QDGTLNIGDP IVVGNTFGRV RAMVNDLGRR VKKVGPSTPV EITGLNDVPQ AGDRFVVFED
EKTARNIGET RASRALVAQR SATNRVSLDN LFEHMKAGEM KEVNVIIKAD VQGSVEALAA
SLRKIDVEGV NVKIIHTAVG AINESDITLA AASNAIVIGF NVRPTAQARE AAENESVDIR
LHRVIYKAID EIEAAMKGML DPEFQEKIIG QAQVRQTINV SKVGTIAGCY VTDGKITRDS
GVRIIRDGIV VFEGEIATLK RFKDDAKEVA KGYECGITVQ NFNDIKEDDV IEAYVMEEIE
RK
