IF2_MOOTA
ID IF2_MOOTA Reviewed; 903 AA.
AC Q2RJM5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Moth_1050;
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Moorella group; Moorella.
OX NCBI_TaxID=264732;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39073 / JCM 9320;
RX PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT thermoaceticum).";
RL Environ. Microbiol. 10:2550-2573(2008).
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; CP000232; ABC19364.1; -; Genomic_DNA.
DR RefSeq; WP_011392564.1; NC_007644.1.
DR RefSeq; YP_429907.1; NC_007644.1.
DR AlphaFoldDB; Q2RJM5; -.
DR SMR; Q2RJM5; -.
DR STRING; 264732.Moth_1050; -.
DR PRIDE; Q2RJM5; -.
DR EnsemblBacteria; ABC19364; ABC19364; Moth_1050.
DR KEGG; mta:Moth_1050; -.
DR PATRIC; fig|264732.11.peg.1130; -.
DR eggNOG; COG0532; Bacteria.
DR eggNOG; COG3170; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
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.
FT CHAIN 1..903
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008277"
FT DOMAIN 403..572
FT /note="tr-type G"
FT REGION 66..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..419
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 437..441
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 458..461
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 512..515
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 548..550
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 104..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 412..419
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 458..462
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 512..515
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 903 AA; 98208 MW; 6E95A71933582A94 CRC64;
MAKTRVYELA KELKVTNKDL IDTMARLGIY TRSHMSVLEN GEVIKVRNHY RQQWRAAKLA
RMHREQATLK GEGPVPTRGV PDAPRAEEVP SRQVPAPETG APAQATGATR QPATGSARPA
NTDETRVQEH KPATAARQAG DAPAAEGTAA AGQPLDGKEL RQAVANGQGT EEPRQQPAAT
GQRAQGGEAG RGQQSRQKKK RRGEGRSRQD ENKGSAREDQ ANRFATRDKE AAPSAGQQSP
AEKGQRRPAH SKPLRIPKPP EAVTKDLPEK RRDRSNARPG AKPAESGRSR KREMENQLEE
RLMRRDKNKG KAQKHKETPK VVFKITLTGS ITVQELAKRI GKTAAEVIKY LMGQGIMATI
NQELDLETAA LVAQDLGAIV EIKAEKPITE LEDLVDPPET LRERPPVVTV MGHVDHGKTS
LLDAIRRTNV TASEAGGITQ HIGAYQVRLK NRKITFLDTP GHAAFTAMRA RGAQATDIAI
LVVAADDGVM PQTIEAINHA KAAGVPIVVA INKIDRPEAN PERVKQQLTE YGLVPEEWGG
DTIMVPVSAV TKEGINDLLE MVLLTADVAE LKANPDRPAR GIVIEAKLDR GRGPVATMLV
QKGTLKIGDN LVAGSVYGRV RAMIDDRGER VNSAPPSTPV EVLGLSELPE AGDIFQVVED
EKLARQIASS RQEEKRQEEL KAASKTTLDD LFKQMEAGEV KELNLVIKGD VQGSVEALRG
ALEQLSTSEV KVNLLHGGVG AITETDVMLA AASKAIIIGF NVRPEANVRK AAEEAGVEIR
LYRVIYEVID DVKAAMSGLL EPEEREVILG RAEVRATFKV PKAGTVAGCF VTEGKIQNRA
LARVIRDGVV VFEGRIESLK RFKDDVREVA QGYECGVGLE KFNDIKEGDV IEAYTIEEIQ
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