IF2_MYCSK
ID IF2_MYCSK Reviewed; 920 AA.
AC A1UER8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Mkms_2128;
OS Mycobacterium sp. (strain KMS).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; unclassified Mycobacterium.
OX NCBI_TaxID=189918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMS;
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 Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL Submitted (DEC-2006) 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; CP000518; ABL91326.1; -; Genomic_DNA.
DR AlphaFoldDB; A1UER8; -.
DR SMR; A1UER8; -.
DR STRING; 189918.Mkms_2128; -.
DR EnsemblBacteria; ABL91326; ABL91326; Mkms_2128.
DR KEGG; mkm:Mkms_2128; -.
DR HOGENOM; CLU_006301_9_2_11; -.
DR OMA; QVRPEMI; -.
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..920
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008282"
FT DOMAIN 416..588
FT /note="tr-type G"
FT REGION 33..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..432
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 450..454
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 475..478
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 529..532
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 565..567
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 88..161
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..225
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 425..432
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 475..479
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 529..532
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 920 AA; 95439 MW; 177F1194F7B978EC CRC64;
MAGKARVHEL AKELGVTSKE LLATLKEQGE FVKSASSTVE APVARRLREK FGSKSAPAPA
KSAGNGATAA PATSATPATA AAAAAPAPAP APQAPAKPAA PKPAAPQPVA PPQPAAAAPT
PPPAASAPAP APAPSAPAPS RPGPTPGPRP GPAPKPAPRT PRVGNNPFST QQPVDRPIPR
PQPRPGAPRP GTPRPGMSPN NMPPRPAGPR PGAPAGRPGG PRPGPGGRGP GGGGGRPGGP
GGGGGGNYRG GGAGGGGGAG GAAAGGFRGR PGGGGRPGQR GGAAGAFGRP GGAPKRGRKS
KRAKRAEYEN MQAPVVGGVR LPHGNGETIR LARGASLSDF AEKINANPAS LVQALFNLGE
MVTATQSVND ETLELLGSEM NYVVQVVSPE DEDRELLESF DLSYGEDAGD EGDLEIRPPV
VTVMGHVDHG KTRLLDTIRQ ANVREGEAGG ITQHIGAYQV LTELDGNERL ITFIDTPGHE
AFTAMRARGA KATDIAILVV AADDGVMPQT VEAINHAQAA DVPVVVAVNK IDKEGADPQK
IRGQLTEYGL IPEEYGGDTM FVDISAKQGT NIDALLEAVL LTADASLDLR ANPDMEAQGV
AIEAHLDRGR GPVATVLIQR GTLRVGDSIV AGDAYGRVRR MVDEHGEDVE AAMPSRPVQV
IGFTSVPGAG DNLLVVDEDR IARQIADRRS ARKRNALAAR SRKRISLEDL DSALKETSQL
NLILKGDNAG TVEALEEALL GIQVDDEVEL RVIDRGVGGV TETNVNLASA SDAIIIGFNV
RAEGKATELA NREGVEIRYY SVIYQAIDEI ESALKGMLKP VYEEKELGRA EIRAIFRSSK
VGNIAGCLVQ SGIMRRNAKA RLLRDNVVVA ENLTVSSLRR EKEDVTEVRD GYECGLTLTY
SDIKEGDVIE TYELVEKART
