IF2_CLAMS
ID IF2_CLAMS Reviewed; 944 AA.
AC B0RDY9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CMS1843;
OS Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM 20744
OS / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum).
OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Clavibacter.
OX NCBI_TaxID=31964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1;
RX PubMed=18192393; DOI=10.1128/jb.01598-07;
RA Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA Parkhill J., Ishimaru C.A.;
RT "Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp.
RT sepedonicus suggests recent niche adaptation.";
RL J. Bacteriol. 190:2150-2160(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; AM849034; CAQ01948.1; -; Genomic_DNA.
DR RefSeq; WP_012299187.1; NZ_MZMN01000003.1.
DR AlphaFoldDB; B0RDY9; -.
DR SMR; B0RDY9; -.
DR STRING; 31964.CMS1843; -.
DR PRIDE; B0RDY9; -.
DR EnsemblBacteria; CAQ01948; CAQ01948; CMS1843.
DR KEGG; cms:CMS1843; -.
DR eggNOG; COG0532; Bacteria.
DR eggNOG; COG3266; Bacteria.
DR HOGENOM; CLU_006301_9_1_11; -.
DR OMA; QVRPEMI; -.
DR Proteomes; UP000001318; 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 PRINTS; PR00315; ELONGATNFCT.
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.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..944
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000075597"
FT DOMAIN 437..611
FT /note="tr-type G"
FT REGION 55..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..453
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 471..475
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 496..499
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 550..553
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 586..588
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 168..182
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 446..453
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 496..500
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 550..553
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 944 AA; 98312 MW; 8364E326DF01FB40 CRC64;
MAKPRVHEIA AEIGVDSKTA LAKLKEMGEF VKGPSSSIEP PVARKLKAAL EAAGVTGQAA
APAAAASSAP RPGARSSAPK PGGRPTPGPQ PTAAPEVEAP EASDVPVPAK PLTVAERQAQ
AEASRKAAAE EKAQAEKSAA SATPEAPAVE TPSAPRPDAG STPAPSNGIP RPGIPRPAAP
RPGNNPFASN QGMGTKPRPG NNPFASNQGM GQRPAAGAAG PRPAAPRPGS PRPGAPRPGG
VGQGARPAGF GQRPAGAGRP GGAPGGAGRP GAPAAGGFQR PAGGFAGRPG GGGRGRGPGG
GTAGAFGRGG GKSKSRKSKR TKRAEFELRE APSLGGVSVP RGDGNTVVRL RRGASISDFA
DKIDASPGNL VTVLFHLGEM ATATESLDEA TFEVLGTELG YKIQVVSPED EDRELLEGFD
IDLDQELEDE DDDVLEIRPP VVTVMGHVDH GKTRLLDAIR NANVIEGEAG GITQHIGAYQ
VWAPHEGYER AITFIDTPGH EAFTAMRTRG AQVTDIAILV VAADDGIMPQ TVEALNHAQA
ANVPIVVAVN KVDKEGANPA KVRQQLTEYG LVAEEYGGDV MFVDVSALTG KGVEDLLEAV
LLTADAGLDL RSNPNKDARG VAIEARLDKG RGAVATVLIQ SGTLRVGDAI VAGTAYGRVR
AMMDENGDAV HEAYPSRPVQ VQGLSSVPGA GDTFLVTEED RTARQIAEKR EAVERNAQLA
KARKRISLED FTRALEEGKV ESLNLIIKGD VSGAVEALEE SLMKIEVDDS VQLRIIHRGV
GAVTESDVNL ATIDNAIIIG FNVRPDPKAR ARAAREGVDI RFYSVIYSAL EEIESSLTGM
LKPEFEEVQS GVAEIREVFR SSKFGNIAGV IVRSGTITRN AKARVIRDGV VVGDSLAIES
LRRFKDDVSE VRTDFEAGIG LGKFNDIQIG DEIETIEMKE KPRG
