IF2_LISIN
ID IF2_LISIN Reviewed; 782 AA.
AC Q92C29;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=lin1362;
OS Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=272626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-680 / CLIP 11262;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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; AL596168; CAC96593.1; -; Genomic_DNA.
DR PIR; AI1602; AI1602.
DR RefSeq; WP_010991496.1; NC_003212.1.
DR AlphaFoldDB; Q92C29; -.
DR SMR; Q92C29; -.
DR STRING; 272626.lin1362; -.
DR EnsemblBacteria; CAC96593; CAC96593; CAC96593.
DR KEGG; lin:infB; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002513; 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; 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_0000137217"
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; 84977 MW; C20CC36B236E98B8 CRC64;
MSKVRVYEYA KEHQVSSKKV IEALKDLGIE VANHMSTINE NALRQLDNAI DGTNKKAEAP
KKETTSNENG NSKGPNKPNM TNSNEKSNKP NKPAGQANKP ATANKSHGAK PATNKPANTS
NQTQSSGNKQ PAGGQKRNNN 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 AASNAIIIGF NVRPTTQARE AAENESVDIR
LHRVIYKAID EIEAAMKGML DPEFQEKIIG QAQVRQTINV SKVGTIAGCY VTDGKITRDS
GVRIIRDGIV VFEGEIATLK RFKDDAKEVA KGYECGITVQ NFNDIKEDDV IEAYVMEEIE
RK
