IF2_HAEIN
ID IF2_HAEIN Reviewed; 829 AA.
AC P44323;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Translation initiation factor IF-2;
GN Name=infB; OrderedLocusNames=HI_1284;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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; L42023; AAC22933.1; -; Genomic_DNA.
DR PIR; E64114; E64114.
DR RefSeq; NP_439436.1; NC_000907.1.
DR RefSeq; WP_010869172.1; NC_000907.1.
DR AlphaFoldDB; P44323; -.
DR SMR; P44323; -.
DR STRING; 71421.HI_1284; -.
DR EnsemblBacteria; AAC22933; AAC22933; HI_1284.
DR KEGG; hin:HI_1284; -.
DR PATRIC; fig|71421.8.peg.1336; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR PhylomeDB; P44323; -.
DR BioCyc; HINF71421:G1GJ1-1310-MON; -.
DR Proteomes; UP000000579; 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; 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..829
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137207"
FT DOMAIN 328..498
FT /note="tr-type G"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..344
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 362..366
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 384..387
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 438..441
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 474..476
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 337..344
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 384..388
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 438..441
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 829 AA; 90552 MW; 75B20AC4CF610AF7 CRC64;
MTEDVKADAP KKLSIQRRTK TTVSSTTTGG KSKEVQVEVR KKRTVKTDIA QQEEAKLKAQ
QEAEAKKIAE QKAAEEKARL EAEKAKAETA KPVKSAVDSK AKSVESEKEK RKAGEAELRR
KAEELARQKA EEQARRAVEE AKRYAEADDS DNESSSEDYS DYNLSSRYAL EAEDEEDRRN
ENRGRGKNKV AKAKKGGRDD ENSKNSKNER ESNRKNQKDA KFGKGKNGKK GAALQQAFTK
PAQVVKSDVV IGETITVAEL ANKMAVKATE IIKMMMKMGE MVTINQVIDQ ETAQLVAEEL
GHKVILRNEN ELEEAVLGDR DVNAEKVTRA PVVTIMGHVD HGKTSLLDYI RKAKVAAGEA
GGITQHIGAY HVEMDDGKMI TFLDTPGHAA FTSMRARGAK ATDIVVLVVA ADDGVMPQTI
EAIQHAKAAG APLVVAVNKI DKPEANLDRV EQELLQHDVI SEKFGGDVQF VPVSAKKGTG
VDDLLDAILL QSEVLELTAV KDGMASGVVI ESYLDKGRGP VATILVQSGT LRKGDIVLCG
FEYGRVRAMR DENGKEVDEA GPSIPVELLG LSGVPAAGDE ATVVRDEKKA REVALYRQGK
FREVKLARQQ KAKLENMFSN MSEGDVAELN VIVKADVQGS VEAIVQALNE LSTNEVKVKV
VGSGVGGITE TDATLATASN AIIVGFNVRA DATARRVIEA ENIDLRYYSI IYELLNEIKA
AMSGMLEPEF KQEIIGLAEV RDVFRHPKFG AIAGCMVTEG VVKRNNPIRV LRDNVVIFEG
ELESLRRFKD DVSEVRNGME CGIGVKNYND VKVGDQIEVF EVVEVKRSI
