IF2_NITSB
ID IF2_NITSB Reviewed; 843 AA.
AC A6Q226;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=NIS_0421;
OS Nitratiruptor sp. (strain SB155-2).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Nautiliales;
OC Nitratiruptoraceae; Nitratiruptor; unclassified Nitratiruptor.
OX NCBI_TaxID=387092;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB155-2;
RX PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA Horikoshi K.;
RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT emergence of pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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; AP009178; BAF69535.1; -; Genomic_DNA.
DR RefSeq; WP_012081798.1; NC_009662.1.
DR AlphaFoldDB; A6Q226; -.
DR SMR; A6Q226; -.
DR STRING; 387092.NIS_0421; -.
DR PRIDE; A6Q226; -.
DR EnsemblBacteria; BAF69535; BAF69535; NIS_0421.
DR KEGG; nis:NIS_0421; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_4_1_7; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001118; 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; IPR004161; EFTu-like_2.
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; PF03144; GTP_EFTU_D2; 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; Reference proteome.
FT CHAIN 1..843
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008289"
FT DOMAIN 342..511
FT /note="tr-type G"
FT REGION 55..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..358
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 376..380
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 397..400
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 451..454
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 487..489
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 61..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 351..358
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 397..401
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 451..454
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 843 AA; 93415 MW; 1AC98E7E2CBC0C9E CRC64;
MDKVRIHEIA SELGLKSKDV LQKAQEMGLK VKSPSSGVSF EEAEKLTDYI INGPAEAVAA
KPQEKPKKSA PKKEEKPKEE VKKEAEEKVA ASKKEEEKPQ EKKSVEESLT PPSLKKRRGL
VIVKKKRPKV EPKVEEKEAK QETPQVTAEE ETPLTLKRKP KKAKKSTPPA KKNEGKKIEI
LEDRDLSDVS MELEEEVVVL PDFSEELQKV EEEQKPKEPQ KKNKQVKVAR KSFAIEQQGI
SRSKKKKRKK KESKSETEIK VVELPEEVRV YEFAEKIGKS VGEVIKVLFN LGMMATKNDF
LDKETLEILA EEFDVEIKIK NVLEELDYVK VYDAVEDDYL EERPPVITIM GHVDHGKTSL
LDYIRNSKIA EREAGGITQH IGAYMIEKDG KRITFIDTPG HEAFTEMRAR GAQATDIAII
VVAADDGVKP QTVEAVNHAK TADVPMIVAI NKIDKPEANP DLVKSQLAEI GITPTEWGGE
YEFVEVSAKT GQGVDDLLDT ILLQAEIMEL KANPKREAKA VVIESSLEKG RGPVATVIVK
NGTLRVGDHV VCGVAFGRVR AIIDDLGKMI KERKPSEPGV VVGLDKVPPA GEILVAVKDA
EEARMYAERR AEYERQKELS KTTKVSLEEL SQLVKEGQLK KLPVIIKADT QGSLEAIKGS
LEKLKNEEVK VDIIHAGVGA ISESDVTLAD ASENAVILGF NVRPTGAVKE KAKQLGVNIK
TYSIIYDLID DVKALLSGML SPIIKEEVIG QAEVRETFNV PKIGTVAGCL VTDGVIERNA
KARVIRDGVV IYDSKISSLK RFKEDVREVT KGYECGLMIE NFNDIKVGDV IEAYKEVEEA
ATL
