IF2_LACP7
ID IF2_LACP7 Reviewed; 1131 AA.
AC A9KNW4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Cphy_2774;
OS Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
OS (Clostridium phytofermentans).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=357809;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700394 / DSM 18823 / ISDg;
RA Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L.,
RA LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA Bruce D., Detter J.C., Han C., Kuske C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E.A., Richardson P.;
RT "Complete genome sequence of Clostridium phytofermentans ISDg.";
RL Submitted (NOV-2007) 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; CP000885; ABX43134.1; -; Genomic_DNA.
DR RefSeq; WP_012200785.1; NC_010001.1.
DR AlphaFoldDB; A9KNW4; -.
DR SMR; A9KNW4; -.
DR STRING; 357809.Cphy_2774; -.
DR PRIDE; A9KNW4; -.
DR EnsemblBacteria; ABX43134; ABX43134; Cphy_2774.
DR KEGG; cpy:Cphy_2774; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; PRPGYQG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000370; 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..1131
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000075600"
FT DOMAIN 632..801
FT /note="tr-type G"
FT REGION 49..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..648
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 666..670
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 687..690
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 741..744
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 777..779
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 64..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 641..648
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 687..691
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 741..744
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1131 AA; 123782 MW; 43F9290ED20A852E CRC64;
MAKMKIHELA KELGVDNNVI VNFLQSKGSE VKSYRNNIEE KEIDLVRGKF KGSVSSNEPK
SIDNGKASRV EKPEKNNSVT AKADQTPSEP VVHKQRPMTA QGERKNMSEQ NVTTGSTESE
DNIQSVGDRK YQHTDRRPQG NNGEGPQTST NSGDRRPQGQ GSYGDRRPQG QNSGDRRPYN
GDRPQGQNSG DRRPYNGDRP QGQNSGDRRP YNGDRPQGQG NYGDRRPQGQ NSGDRRPYNG
DRPQGQGNYG DRRPQGQGSY GDRRPNSGDR PQGQGNYGDR RPQGQGSYGD RRPQGQGSYG
DRPQGQGSYG DRPQGQGSYG DRRPQGQGSY GDRRPQGQGS YGDRPQGQGS YGDRRPQGQG
SYGDRPQGQG NYGDRRPGGQ GSYGDRRPQG QGSYGDRPQG QGNFGDRRPQ GQGGYGGRPQ
GQGSYGGRPQ GQGGYAGRSQ GQGSFGGFNK DFDKDKDSGY TRSFDKKRTD PKSGEKSSIK
SDLANELTKE QRAAAFNDKS RDRDRNRDRG RNNVEDGNIK SAKGKKDPNR KGAFIMPKPQ
QSLEKQDEIK TVIIPEVLTI KELADKMKVV PSVVVKKLFL AGKMVSINSE ITFEEAEEIA
LGYEIIAEKE VLVNKVEELL KEDDEDENLM VKRPPVVCVM GHVDHGKTSL LDAIREANVT
SREAGGITQH IGAYTVEVNG EKITFLDTPG HEAFTSMRMR GAKSTDIAIL VVAADDGVMP
QTVEAISHAK AAGVQIIVAI NKIDKPSANI ERVKQELTEH ELIAEDWGGD TIFVPVSAHT
KEGIDQLLEM IILTAEMGEL KANPDRMARG IVIEAELDKG RGTVATILVQ KGTLHVGDNI
VIGSTYGKVR AMMDDKGRRV KEATPSTPVE ILGLNAVPNA GEIFMATENE KEARNIADAF
ISQGKERLLA DTKAKLSLDG LFSQIQAGNI KELNLIVKAD VQGSVEAVKQ SLVKLSNEEV
AVRIIHGGVG AINESDVMLA STSNAIIIGF NVRPDNMARE IAEREKVDLR LYRVIYSAIE
DVEAAMKGML DPTFEEKVMG HAEVRQVFKA SGLGTIAGSY VLDGKIVRGC SARITREGTQ
IFEGALASLK RFKDDVKEVN TGYECGLVFE KFNDIQEYDL VELYMMVEVP R
