IF2_EHRCR
ID IF2_EHRCR Reviewed; 842 AA.
AC Q2GGQ8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
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=ECH_0563;
OS Ehrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=205920;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC CRL-10679 / Arkansas;
RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C.,
RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C.,
RA Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D.,
RA Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT "Comparative genomics of emerging human ehrlichiosis agents.";
RL PLoS Genet. 2:208-222(2006).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABD44916.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000236; ABD44916.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_044148381.1; NC_007799.1.
DR AlphaFoldDB; Q2GGQ8; -.
DR SMR; Q2GGQ8; -.
DR STRING; 205920.ECH_0563; -.
DR EnsemblBacteria; ABD44916; ABD44916; ECH_0563.
DR KEGG; ech:ECH_0563; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_2_5; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000008320; 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; 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; 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..842
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335467"
FT DOMAIN 340..510
FT /note="tr-type G"
FT REGION 121..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..356
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 374..378
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 396..399
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 450..453
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 486..488
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 126..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 349..356
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 396..400
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 450..453
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 842 AA; 93191 MW; 5A0AD4E643A9D142 CRC64;
MNESKSVVDS GLMSGKIERT TLKLSDKLKL SSNIHQGTKF SLKKSVTTVE VRKSKKRKDI
NNIEQASVVL QNDNAYQDNE SNNSLTIQEQ ISRMNALQNA NICEKKEDIK EDTSDVNLQV
TESTSVEKSE SDDVTLEEES SKKVEEQVVE EAHDNTDTVS LNVVENVQEE SQVDNQVESS
NISDILQPKG IEEKKLKKYE KEHEEKKGNP KKGVSNNMYS KHVKLVIEEE LEDNNKQVIQ
THKSRKNRST SSVKNKITRK VLIPKKITVQ ELASSMSERV KDVQHMLFQM GRRDIKPTDF
LDSDHASVIV EAFNHTFKLV NDGKLEEDLY ADGNDKELLP RAPVVTVMGH VDHGKTSLLD
AIRKSNVADG EFKGITQHIG AYQIMLDGDK RITFIDTPGH EAFTAMRACG TNVTDIVVLV
VAADDGIMPQ TIESINHVKA ANVAMIVAVN KIDKHDANID KITNSLLNHG VVAESLGGDV
IVVPVSAKER INLDQLKSSI LLMAELLELK AVYDTRASGV VIESKVDRNC GVVATLIVQK
GTLKAGDIIV VGHNSYGKVR NMFNSDGRSE KVAIPSMPVK VLGLNNVPNS GTNFIVVDSE
KQARELISYR QELFNAELEA NAKPKMDANS ILACGVVDEL NVILKCDVMG SVEAICYSIS
KITHEDIKLN VLYKGVGNVT KSDVLLAETS NSIILAFNVK TDASVKELAK QKCIEIKHYS
VIYDIIDDVK KILSSMLKPL QQEVQVGTLS IRKVFSSGSI GSVLGCYVTN GIVRKGALVK
LIRNNNVIHE GKIKVLRRFK DDVKEVAAGF ECGILLDYSK EIYPESDIIH ILEIVEEIRV
IK
