IF2_NITHX
ID IF2_NITHX Reviewed; 868 AA.
AC Q1QS64;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Nham_0031;
OS Nitrobacter hamburgensis (strain DSM 10229 / NCIMB 13809 / X14).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Nitrobacter.
OX NCBI_TaxID=323097;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10229 / NCIMB 13809 / X14;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Ward B., Arp D., Klotz M., Stein L.,
RA O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T.,
RA Gentry M.E., Bruce D., Richardson P.;
RT "Complete sequence of chromosome of Nitrobacter hamburgensis X14.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000319; ABE60933.1; -; Genomic_DNA.
DR RefSeq; WP_011508640.1; NC_007964.1.
DR AlphaFoldDB; Q1QS64; -.
DR SMR; Q1QS64; -.
DR STRING; 323097.Nham_0031; -.
DR EnsemblBacteria; ABE60933; ABE60933; Nham_0031.
DR KEGG; nha:Nham_0031; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_2_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001953; 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..868
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008288"
FT DOMAIN 365..535
FT /note="tr-type G"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 28..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..381
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 399..403
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 421..424
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 475..478
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 511..513
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 41..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 374..381
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 421..425
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 475..478
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 868 AA; 93501 MW; 8CCA8FA9CA43480D CRC64;
MVDTKNPGDK TLSVGPSKTL TLKPRVEQGT VRQSFSHGRT KQVVVEKRGK RRIGGDAPAA
EPVAASEPTV ARAPRIPVRP APPAASRANS GVVLRTLTED ERTARASALA EAKIRAEEER
RIAEAEAARR NSKEGIEQAE REAAEARRKA EEERHRQEEE AKRKAELEAK RRFGESETKA
APAKTTTTTT RAAPPARPAA VAADGSDEEE APRLVRRPGG GPARPVVAPK PAAKPAPAKQ
RGRLTLVTAL SADDVRERSI ASFRRRTQRL KGHASNEPKE KLIREVIVPE AITIQELANR
MAERAVDVIR MLMKQGAMHK ITDVIDADTA QLIAEELGHT VKRVAASDVE EGLFDADDDS
TVVEPRSPVV TVMGHVDHGK TSLLDAVRHA NVVSGEAGGI TQHIGAYQVT SPDGKKITFI
DTPGHAAFTA MRARGAKVTD IVVLVVAADD GVMPQTVEAI NHAKAAKVPM IIAINKIDKP
DAKPERVRTE LLQHEVQVES MGGQVIDVEV SAKNKTNLDK LLEMISLQAD LLDLKTNASR
PAEGTVIEAK LDRGRGPVAT VLVQRGTLRV GDIIVAGAEM GRVRALISDQ GETVDEAGPS
VPVEVLGFNG PPEAGDRLAV VENEARARQV TSYRAHQKRE NAAASSSGMR GSLEQMMSQL
KTAGRKDFPL VIKADVQGSL EAILGSLEKL GTEEVAARIL HAGVGGISES DVTLAEGFNA
AIIGFSVRAN KEAAAAAKRN GIEIRYYNII YDLVDDVKKA MSGLLAPTLR ETMLGNAEIL
EVFNISKVGK VAGCRVTDGN VERGANVRLI RENVVVHEGK LSTLKRFKDE VKEVQSGQEC
GMAFESYHDM RVGDVIECYR VETIQRSL
