IF2_MYCA9
ID IF2_MYCA9 Reviewed; 912 AA.
AC B1MD87;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=MAB_3131c;
OS Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CIP 104536 / JCM
OS 13569 / NCTC 13031 / TMC 1543) (Mycobacterium abscessus).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacteroides; Mycobacteroides abscessus.
OX NCBI_TaxID=561007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC
RC 1543;
RX PubMed=19543527; DOI=10.1371/journal.pone.0005660;
RA Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M.,
RA Macheras E., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L.,
RA Gaillard J.L.;
RT "Non mycobacterial virulence genes in the genome of the emerging pathogen
RT Mycobacterium abscessus.";
RL PLoS ONE 4:E5660-E5660(2009).
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; CU458896; CAM63208.1; -; Genomic_DNA.
DR RefSeq; WP_012296639.1; NZ_MLCG01000003.1.
DR AlphaFoldDB; B1MD87; -.
DR SMR; B1MD87; -.
DR PRIDE; B1MD87; -.
DR EnsemblBacteria; CAM63208; CAM63208; MAB_3131c.
DR GeneID; 66968554; -.
DR KEGG; mab:MAB_3131c; -.
DR OMA; QVRPEMI; -.
DR Proteomes; UP000007137; 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..912
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093804"
FT DOMAIN 408..579
FT /note="tr-type G"
FT REGION 26..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..424
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 442..446
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 467..470
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 521..524
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 557..559
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 97..120
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..154
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..216
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 417..424
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 467..471
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 521..524
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 912 AA; 94773 MW; 045A4BC10342321A CRC64;
MAGKARVHEL AKELGVTSKE VLARLSDQGE FVKSASSTVE APVARRLRES FGGGDKPAPA
ASNGAAAEAA APPKKAGPKP GAPKPAPKKV AEPVVEAPVA PEPPAAPAAP AAPAPKPSPA
ARPAAAEAAA PAPAPAPAPR PGATPGPKPG APRVPRVGNN PFSSAQPAER PAPRPQAPRP
GAPRPGGASP SNMPPRPSPG SMGPRPPRPG GGPRPGGGPR PGGAGRPGGG GGGNYRGGGT
GTGAPAGGPP GAGGGFRGRP GGGGGGGRPG QRGGAAGAFG RPGGAPKRGR KSKRAKRAEY
ENMQAPVVGG VRLPHGNGEV IRLARGASLS DFAEKIDANP ASLVQALFNL GEMVTATQSV
GDETLELLGG EMNYVVQVVS PEDEDRELLE SFDLTYGEDE GGEEDLRTRP PVVTVMGHVD
HGKTRLLDTI RKANVREGEA GGITQHIGAY QVAVEHDGTE RPITFIDTPG HEAFTAMRAR
GAKATDIAIL VVAADDGVMP QTVEAINHAQ AADVPIVVAV NKIDKEGADP AKIRAQLTEY
NLVAEDFGGD TMFVDISARQ GTNIEQLLEA VLLTADAALD LRANPDMEAQ GVAIEAHLDR
GRGPVATVLI QRGTLRVGDS IVAGDAYGRV RRMVDEHGED VEEALPSRPV QVIGFTSVPG
AGDNLLVVDE DRIARQIADR RSARKRNALA ARSRKRISLD DLDAALKETS QLNLILKGDN
AGTVEALEEA LLGIAIDDEV QLRVIDRGVG GVTETNVNLA SASDAIIIGF NVRAEGKATE
LANREGVDIR YYSVIYQAID EIESALKGML KPVYEEVELG RAEIRAMFRS SKVGNIAGCL
VTSGIIRRNA KARLLRDNIV VAETVTISSL RREKDDVVEV RDGYECGLTL TYNDIKEGDV
IEAYELREKE RV
