IF2_ALKEH
ID IF2_ALKEH Reviewed; 883 AA.
AC Q0A797;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Mlg_1948;
OS Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Alkalilimnicola.
OX NCBI_TaxID=187272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1101 / DSM 17681 / MLHE-1;
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 Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S.,
RA Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B.,
RA Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P.;
RT "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL Submitted (AUG-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; CP000453; ABI57290.1; -; Genomic_DNA.
DR RefSeq; WP_011629684.1; NC_008340.1.
DR AlphaFoldDB; Q0A797; -.
DR SMR; Q0A797; -.
DR PRIDE; Q0A797; -.
DR EnsemblBacteria; ABI57290; ABI57290; Mlg_1948.
DR KEGG; aeh:Mlg_1948; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001962; 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; 1.
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..883
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008194"
FT DOMAIN 383..550
FT /note="tr-type G"
FT REGION 52..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..399
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 417..421
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 438..441
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 492..495
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 528..530
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 52..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 392..399
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 438..442
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 492..495
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 883 AA; 96386 MW; EED00FE21843F9FC CRC64;
MAEDKVREFA ETVGIPVERL VSQLEAAGIS GRGPEDPLSD LDKATLLEYL RKGRDGGEQD
DDQAPSKITL RRKKVSTLKM PASGGGGSGA RGPRQTRTVN VEVRKKRTYV KRSVVEAEES
KHDVERLERA LIEDRKRAEE RARREAEEAE ARRREQEEAE RRQAEAEALR QAEAEREATA
ETAGVADEAD KAEPQPDPEA ARLAAEKEEA RRREEEKERR RLEQEARRER EAEERAARKT
GATAPAAKGK QKKGRESLSM GAGKPGRRGG KKGGRRAASG GEAAKQLQHG FAKPTQPVVR
EVEIPESITV GDLAQKMSVK AAVLIKEMMK QGVMATINQA LDQDTAVLLV EEMGHKPVIV
RADALEEEVL QDTSQAQEGD KAPRPPVVTV MGHVDHGKTS LLDNIRRAKV ADAEAGGITQ
HIGAYHVETD RGMVTFLDTP GHEAFTAMRA RGAQLTDIVV LVVAADDGVM PQTEEAVRHA
KAAEVPMVVA VNKIDKPDAD PDRVKQELSQ MEVIPEEWGG DVQFIHVSAK QGEGLDDLLE
AILLQAELME LGAVAEGNAS GIVLESSLDK GRGPVATVLV QSGLLKKGDS LLCGTEYGRV
RALIDETGKR VDEAGPSIPV VVLGLSGLPS AGDDMVVVDD EKKAREVAEM RKERQRDKRL
AQQQAARMEN LFNQMKEDEV NTVNLVVKAD VQGSAEALQQ SLANLSTDDI QVKVISSGVG
AINESDVNLA LASNAILIGF NVRADAAARR LVQENDVDLH YYSVIYDAIE QVKNAISGML
EPELEEHIIG LAEVKDVFRS SKLGAVAGCL VTEGAVRRKN PIRVLRDNVV IYEGELESLR
RHKDDVTEVK SGTECGIGVK NYNDVRIGDQ IECYERVEVR REL
