IF2_CLAM3
ID IF2_CLAM3 Reviewed; 944 AA.
AC A5CSZ4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CMM_2149;
OS Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382).
OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Clavibacter.
OX NCBI_TaxID=443906;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 382;
RX PubMed=18192381; DOI=10.1128/jb.01595-07;
RA Gartemann K.-H., Abt B., Bekel T., Burger A., Engemann J., Fluegel M.,
RA Gaigalat L., Goesmann A., Graefen I., Kalinowski J., Kaup O., Kirchner O.,
RA Krause L., Linke B., McHardy A., Meyer F., Pohle S., Rueckert C.,
RA Schneiker S., Zellermann E.-M., Puehler A., Eichenlaub R., Kaiser O.,
RA Bartels D.;
RT "The genome sequence of the tomato-pathogenic actinomycete Clavibacter
RT michiganensis subsp. michiganensis NCPPB382 reveals a large island involved
RT in pathogenicity.";
RL J. Bacteriol. 190:2138-2149(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; AM711867; CAN02219.1; -; Genomic_DNA.
DR RefSeq; WP_012038839.1; NC_009480.1.
DR AlphaFoldDB; A5CSZ4; -.
DR SMR; A5CSZ4; -.
DR STRING; 443906.CMM_2149; -.
DR EnsemblBacteria; CAN02219; CAN02219; CMM_2149.
DR KEGG; cmi:CMM_2149; -.
DR eggNOG; COG0532; Bacteria.
DR eggNOG; COG3266; Bacteria.
DR HOGENOM; CLU_006301_9_1_11; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001564; 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.
FT CHAIN 1..944
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008228"
FT DOMAIN 437..611
FT /note="tr-type G"
FT REGION 55..329
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; 98307 MW; 7C8AF45F449CA8C5 CRC64;
MAKPRVHEIA AEIGVDSKTA LAKLKEMGEF VKGPSSSIEP PVARKLKAAL EAAGLTGQAA
APAAAPSSAP RPGARSSAPK PGGRPTPGPQ PTAAPEVEAP EASDVPVPAK PLTVAERQAQ
AEASRKAAAE EKAQAEKSAA SATPDAPAAE TPSAPRPDAG SAPAPSNGIP RPGIPRPAAP
RPGNNPFASN QGMGTKPRPG NNPFASNQGM GQRPAAGAAG PRPAAPRPGS PRPGAPRPGG
VGQGARPAGF GQRPAGAGRP GGAPGGAGRP GAPAAGGFQR PAGGFAGRPG GGGRGRGPGG
GTAGAFGRGG GKSKSRKSKR TKRAEFELRE APSLGGVSVP RGDGNTIVRL RRGASISDFA
DKIDASPGNL VTVLFHLGEM ATATESLDEA TFEVLGTELG YKIQVVSPED EDRELLEGFD
IDLDQELEDE DDDVLEIRPP VVTVMGHVDH GKTRLLDAIR NANVIEGEAG GITQHIGAYQ
VWAPHEGYER AITFIDTPGH EAFTAMRARG 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 KPRV
