IF2_PASMU
ID IF2_PASMU Reviewed; 833 AA.
AC P57873;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Translation initiation factor IF-2;
GN Name=infB; OrderedLocusNames=PM0759;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AE004439; AAK02843.1; -; Genomic_DNA.
DR RefSeq; WP_005726750.1; NC_002663.1.
DR AlphaFoldDB; P57873; -.
DR SMR; P57873; -.
DR STRING; 747.DR93_1594; -.
DR EnsemblBacteria; AAK02843; AAK02843; PM0759.
DR KEGG; pmu:PM0759; -.
DR PATRIC; fig|272843.6.peg.768; -.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000000809; 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..833
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137230"
FT DOMAIN 333..502
FT /note="tr-type G"
FT REGION 1..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..349
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 367..371
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 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 342..349
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 388..392
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 442..445
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 833 AA; 90862 MW; 381F1113E2D2C897 CRC64;
MTEDVKKADG AAPKKLSLQR RTKTTVSTTA GGKAKEVQVE VRKKRTVPTD AAQKAEEARL
KAKQEADRLA AEKAKKDAEE KARLEAEKAK QAKAEEAKKA QAVSAPTKAV DVEKEKRRAE
EAELRRKADE LARQKAEELA RKAAEEAKRY AELSEEDAEN ENSEDYADYH LTSTYAREAE
DEEARRKENR NRGGKNKVAK AKKGGREDES SKTERESNRR NQKDGKMGKG KHAKKGSALQ
QAFTKPAQAV NRDVVIGETI TVAELANKMA VKATEVIKTM MKMGAMATIN QVIDQETAQL
VAEEMGHKVI IRKENELEES VMSDRDVDAE LVTRAPVVTI MGHVDHGKTS LLDYIRKAKV
ASGEAGGITQ HIGAYHVETD GKMITFLDTP GHAAFTSMRA RGAKATDIVV LVVAADDGVM
PQTIEAIQHA KAAGVPIVVA VNKIDKPEAN PERVETELLQ HEVVAEKFGG DTQFVYVSAK
KGTGVDELLE AILLQSEVLE LTAVKDGMAT GVVIESYLDK GRGPVATILV QTGTLHRGDI
VLCGFEYGRV RAMRNENGKD VASAGPSIPV EVLGLSGVPA AGDEATVVRD EKKAREVALY
RQGKFREVKL ARQQKAKLEN MFTNMAEGDV AELNVIVKAD VQGSVEAICQ SLNELSTAEV
KVKVVGSGVG GITETDATLA AASNAIVLGF NVRADASARR IIESESIDLR YYSIIYELLN
EIKAAMSGML QPEFKQEIIG LAEVRDVFRH PKFGAIAGCM VTEGIVKRNN PIRVLRDNVV
IFEGELESLR RFKDDVAEVR NGMECGIGVK NYNDVKVGDQ IEVFEVVEIK RTI
