IF2_LACE2
ID IF2_LACE2 Reviewed; 939 AA.
AC C4Z5N7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN OrderedLocusNames=EUBELI_00894;
OS Lachnospira eligens (strain ATCC 27750 / DSM 3376 / VPI C15-48 / C15-B4)
OS (Eubacterium eligens).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lachnospira.
OX NCBI_TaxID=515620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27750 / DSM 3376 / VPI C15-48 / C15-B4;
RX PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA Hettich R.L., Gordon J.I.;
RT "Characterizing a model human gut microbiota composed of members of its two
RT dominant bacterial phyla.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(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; CP001104; ACR71896.1; -; Genomic_DNA.
DR RefSeq; WP_012739132.1; NC_012778.1.
DR AlphaFoldDB; C4Z5N7; -.
DR SMR; C4Z5N7; -.
DR STRING; 515620.EUBELI_00894; -.
DR EnsemblBacteria; ACR71896; ACR71896; EUBELI_00894.
DR GeneID; 41355629; -.
DR KEGG; eel:EUBELI_00894; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NQNRDGQ; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001476; 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; 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..939
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000202772"
FT DOMAIN 440..609
FT /note="tr-type G"
FT REGION 48..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..456
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 474..478
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 495..498
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 549..552
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 585..587
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 61..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 449..456
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 495..499
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 549..552
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 939 AA; 103788 MW; A1AD7AE1A4EC1327 CRC64;
MANMRVHELA KELNITSKDI TDMLSNSEKT YKPVSGLTDA EISSVRKKFA PAPKVENKPA
AQPAKQSQPV KNDNRDNRQQ NQAPKQPQQG TQNKSGNADD KKHISQVYFP QNSSRDKNSR
RDNNNRDGQR DNNGGYRNND RNNGGYRNND RGNNGYRNND RNNNGGYGNR DNNGGYRNND
RNNNGGYGNR DNNGGYRNND RNNGGYRNND RNNNGGYGNR DNNGGYRNND RNNNGGYGNR
DNNGGYRNND RNNNGGFRND RNGQSGNGGF RKDNDQNRGG FNGGQRRNND RRDSAPKEEF
DFSAKPDSRR HDSRIDSKKN DRKRDNEAKE NLKFANSRFD KKPMTKPEKK EKEEETIKQL
VLPDTLTIKE LADKMKVAPA ALVKKLFLQG KVVTINEEID YDAAEEIALE FNCICEHEEK
VDVIAELLKE DEEPEDKLVP RPPVVCVMGH VDHGKTSLLD AIRETHVTAK ESGGITQKIG
AYQVNVNGNL ITFLDTPGHE AFTAMRMRGA QATDIAILVV AADDGVMPQT IEAINHAKAA
GVEIIVAVNK IDKPNANIEK VKQELTEYGL IAEDWGGSTT FVPVSAHTKQ GIDELLDMIL
LTAEVNELKA NPDRKARGIV IEAELDKGRG PVASILVQKG TLHVGDAVSA GSCYGKIRAM
IDDKGNRVKV AGPSTPVEIL GLNDVPNAGE IIMAADSEKE ARSIAETFIS EGRKKLLDDT
KHKVSLDALF EQIQAGNMKE LNIIIKADVQ GSVEAVKSSL VRLSNEEVVV KVIHGGVGNV
NESDVVLASA SNAIIIAFNV KPDNQARIVA EREKVDLRLY SVIYNAIEDV EAALKGMLEP
IYEEKIIGHA RIMQIFKASG VGNIAGCIVE EGRITRDSVV RITRGSEKVY EGPIASLKHF
KDEVKEIKAG TECGMVFEKF NDIQPEDMIE AHIMVEVPR
