IF2_ACET2
ID IF2_ACET2 Reviewed; 1035 AA.
AC A3DE44;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Cthe_0991;
OS Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=203119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC B-4536 / VPI 7372;
RG US DOE Joint Genome Institute;
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 Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA Newcomb M., Richardson P.;
RT "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL Submitted (FEB-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000568; ABN52223.1; -; Genomic_DNA.
DR AlphaFoldDB; A3DE44; -.
DR SMR; A3DE44; -.
DR STRING; 203119.Cthe_0991; -.
DR EnsemblBacteria; ABN52223; ABN52223; Cthe_0991.
DR KEGG; cth:Cthe_0991; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NNQRSDR; -.
DR Proteomes; UP000002145; 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..1035
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000057653"
FT DOMAIN 537..706
FT /note="tr-type G"
FT REGION 56..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..553
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 571..575
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 592..595
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 646..649
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 682..684
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 114..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 546..553
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 592..596
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 646..649
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1035 AA; 114956 MW; D7A08699EFA6C4E2 CRC64;
MAKKRVYELA KELNTTSKRL MEKLEEINIV VKNHMSFLEE DELEALYDHI GVIRHKDDKS
NTDDNKTASA HSVAQHSSEA MKELKKEAKK APRIIRTTEI YLDSKDEEIK EIKANDAKSQ
KKPEEKRKKN DFVRVETETS GLRPGLVRET KPEYMRILEE QKKSEASKAQ TNEKKDAEKN
SVKEVVKKEE GSKQTAEIKD GSVNMEGKVL EEVKATVADS ATNVNLNESI DKDKKTNDNR
QVSTDNSAVN NEENAADTLN KKDMDKKNNN KKNEAKKNAE KKNEAKKNEK NDNKGGNAKK
NEHRSPDMKK NDSNRPQDAN KQNSKAAADK NREEGRTGSK KSLEIPKVEL TTSQKEEFNS
QRAERREYNK DAEKDSKREL RKEQPRSAIS GGRNKNHKVI KNVFNSRKGV SEVLSDDFEM
DDFYFGGSKK SRKIKKKKEE KKEEKPAPPK PVVTSIKIAA PITVKELAEA LKKTSAEVIK
KLMSLGIMAT LNQELDFDTA AIVADEFGVK AEEEVVVNEE DILFDDSDDP NDPEAVPRPP
VVVVMGHVDH GKTSLLDAIK KTNVTEKEAG GITQHIGAYM VKINNRNITF LDTPGHEAFT
AMRARGAQVT DIAVLVVAAD DGVMPQTIEA INHAKAANVT IIVAINKIDK PTANPEKVKQ
ELTEYGLIPE EWGGDTIFVE VSAKKGVNID YLLEMILLAA DMLELKANPN KQAKGTVIEA
KLDKDKGPVA TVLVQRGTLC VGDSIIVGTT TGRIRAMTDD KGHRIKKAGP STPVEILGLH
EVPEAGETFY VITDEKTAKQ LIEKRKLKQR EQLLKASARV TLDDLFNQIK EGKVKELNII
VKADVQGSVE ALKQSLEKLS NDEVRVKIIH GGVGSVTETD VTLAQVSNAI IIGFNVRPPA
NVIDAAKKAG VDLRLYTIIY NAIEDIEAAM KGMLEPTYKE VVIGHVEIRQ IFKVSGVGTV
GGGYVTDGKI TRNANIRLVR DGIVVHEGKL GSLKRFKDDV REVAEGYECG LSIEKFNDIK
EGDVVEVYVM EEVKE
