IF2_LARHH
ID IF2_LARHH Reviewed; 959 AA.
AC C1D8X2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=LHK_01928;
OS Laribacter hongkongensis (strain HLHK9).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Laribacter.
OX NCBI_TaxID=557598;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLHK9;
RX PubMed=19283063; DOI=10.1371/journal.pgen.1000416;
RA Woo P.C.Y., Lau S.K.P., Tse H., Teng J.L.L., Curreem S.O., Tsang A.K.L.,
RA Fan R.Y.Y., Wong G.K.M., Huang Y., Loman N.J., Snyder L.A.S., Cai J.J.,
RA Huang J.-D., Mak W., Pallen M.J., Lok S., Yuen K.-Y.;
RT "The complete genome and proteome of Laribacter hongkongensis reveal
RT potential mechanisms for adaptations to different temperatures and
RT habitats.";
RL PLoS Genet. 5:E1000416-E1000416(2009).
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; CP001154; ACO74912.1; -; Genomic_DNA.
DR RefSeq; WP_012697398.1; NC_012559.1.
DR AlphaFoldDB; C1D8X2; -.
DR SMR; C1D8X2; -.
DR STRING; 557598.LHK_01928; -.
DR PRIDE; C1D8X2; -.
DR EnsemblBacteria; ACO74912; ACO74912; LHK_01928.
DR KEGG; lhk:LHK_01928; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002010; 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; IPR009061; DNA-bd_dom_put_sf.
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; 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; Reference proteome.
FT CHAIN 1..959
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000118764"
FT DOMAIN 459..628
FT /note="tr-type G"
FT REGION 55..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..475
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 493..497
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 514..517
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 568..571
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 604..606
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 55..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 468..475
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 514..518
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 568..571
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 959 AA; 102235 MW; 6A59328C17B750A3 CRC64;
MQEMNVKQFA GELKMQPEHL LEQLKSAGVN KTSINDALSH VDKERLLDFL RQGRNEGGRV
TLKRKETSEV RANDASGRSR TIQVEVRKKR VLERPAEAAR PAAAPAVAQE APAAEMREPE
ARPQAPAAEP ALKPADRVGA PAVRTERKPE PKPEPAKAEP ARAAKPEPKP EPVKAEPAKA
VAEPAPAAEA TQPAAAPARP VSILSAEEIA SREAEERRQA ELRARQEALI RERQEREARR
MAAKLAAQQK AQEAANPKPA AEKPAESRPA RPAEGRSGAR PAPAARPAAG GARPAPAAGA
PAGAARPAGS GADDRRGAGK KTGGGNTDRD GGKKRGGLKT RGGDASSGWK SGSRKGKRQH
QDNQHAFQAP AEPIVHEVMV PETITVADLA HKMAVKAAEV IKALMKMGMM VTINQVLDQE
TALIVVEELG HIGKAAKTDD PEAYLDVEDG NVVEAKLEHR APVVTVMGHV DHGKTSLLDR
IRKAKVAAGE AGGITQHIGA YHVDTPRGMI TFLDTPGHEA FTAMRARGAK ATDIVVLVVA
ADDGVMPQTI EAIHHAKAAG VPIVVAVNKI DKQGANPERI RQELVAQEVV PEDWGGDTQF
VEVSAKQGLN IDGLLEAILL QAEVLELTAP VDAPAKGIIV EARLDKGRGS VATLLVQSGT
LRKGDVLLAG TAFGRVRAML DEDGKQIEEA GPSIPVEILG LSDVPGAGED AMVLADEKKA
REIANFRAGK YRDVRLAKQQ AAKLENMFAQ MAEGEVRSLP LIIKADVQGS YEALAGSLQK
LSTDEVRVQI LHSGVGGITE SDVNLAAASN AVIIGFNTRA DATARKVAEA NGVDIRYYNV
IYDAIDEVKS ALSGMLAPEK KEEITGTAEV RQLFVVSKVG TIAGCMVIDG MIKRTSRIRV
IRNHVVVHDG ELDSLKRFKD DVKEVKQGYD CGIMLKGFND LLEGDQLEAY EIVEVARSL
