IF2_MYCMM
ID IF2_MYCMM Reviewed; 947 AA.
AC B2HKS2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=MMAR_1894;
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=216594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M;
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(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; CP000854; ACC40343.1; -; Genomic_DNA.
DR AlphaFoldDB; B2HKS2; -.
DR SMR; B2HKS2; -.
DR STRING; 216594.MMAR_1894; -.
DR PRIDE; B2HKS2; -.
DR EnsemblBacteria; ACC40343; ACC40343; MMAR_1894.
DR KEGG; mmi:MMAR_1894; -.
DR eggNOG; COG0481; Bacteria.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_2_11; -.
DR OMA; QVRPEMI; -.
DR Proteomes; UP000001190; 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.
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..947
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093805"
FT DOMAIN 443..614
FT /note="tr-type G"
FT REGION 47..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..459
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 477..481
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 502..505
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 556..559
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 592..594
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 105..127
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..188
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..255
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 452..459
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 502..506
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 556..559
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 947 AA; 98161 MW; 93EA1CDFEE9B81DA CRC64;
MAGKARVHEL AKELGVTSKE VLARLSEQGE FVKSASSTVE APVARRLRES FGGGKSAPAK
GSDTGAAKGV AKAPQKVPGV SPAAKAPDRS LDAALDKAVG NGAPAPVPAP APAPTPAPAP
APAQPADSGV APPAATPAAP AASAAPAPPK APLPGQRPAP TPGKPAAPQA PHPGMAPGAR
PGPVPKPGVR TPRVGNNPFS SAQPVDRPIP RPQAPRPGAP RPGAPRPGGA SPGNMPPRPG
GASGGPRPPR TGAPRPGGGR PGGPGGGRSD GGGGNYRGGG GGVGAAPGGG FRGRPGGGGG
GGRPGQRGGA AGAFGRPGGA PRRGRKSKRA KRAEYENMQA PVVGGVRLPH GNGETIRLAR
GASLSDFADK INANPAALVQ ALFNLGEMVT ATQSVGDETL ELLGSEMNYN VQVVSPEDED
RELLESFDLT YGEDSGDESE LQTRPPVVTV MGHVDHGKTR LLDTIRKANV REGEAGGITQ
HIGAYQVSVD HDGTERLITF IDTPGHEAFT AMRARGAKAT DIAILVVAAD DGVMPQTVEA
INHAQAADVP IVVAVNKIDK EGADPAKIRG QLTEYGLVAE DFGGDTMFVD ISAKQGTNIE
ALEEAVLLTA DAALDLRANP DMEAQGVAIE AHLDRGRGPV ATVLVQRGTL RVGDSVVAGD
AYGRVRRMVD EHGEDVEEAL PSRPVQVIGF TSVPGAGDNF LVVDEDRIAR QIADRRSARK
RNALAARSRK RISLEDLDSA LKETSQLNLI LKGDNAGTVE ALEEALMGIE VDDEVALRVI
DRGVGGITET NVNLASASDA IIIGFNVRAE GKATELANRE GVEIRYYSVI YQAIDEIEKA
LRGMLKPIYE EVELGRAEIR ALFRSSKVGL IAGCMISSGV VRRNAKARLL RDNIVVVENL
SIHSLRREKD DVTEVREGFE CGMTLGYSDL KEGDFIESYE LVQKDRS
