IF2_MICLC
ID IF2_MICLC Reviewed; 930 AA.
AC C5C9T1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Mlut_07010;
OS Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 /
OS NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus lysodeikticus).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Micrococcus.
OX NCBI_TaxID=465515;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC
RC 2665 / VKM Ac-2230;
RX PubMed=19948807; DOI=10.1128/jb.01254-09;
RA Young M., Artsatbanov V., Beller H.R., Chandra G., Chater K.F., Dover L.G.,
RA Goh E.B., Kahan T., Kaprelyants A.S., Kyrpides N., Lapidus A., Lowry S.R.,
RA Lykidis A., Mahillon J., Markowitz V., Mavromatis K., Mukamolova G.V.,
RA Oren A., Rokem J.S., Smith M.C., Young D.I., Greenblatt C.L.;
RT "Genome sequence of the Fleming strain of Micrococcus luteus, a simple
RT free-living actinobacterium.";
RL J. Bacteriol. 192:841-860(2010).
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; CP001628; ACS30233.1; -; Genomic_DNA.
DR RefSeq; WP_012750791.1; NZ_WBMF01000008.1.
DR AlphaFoldDB; C5C9T1; -.
DR SMR; C5C9T1; -.
DR STRING; 465515.Mlut_07010; -.
DR PRIDE; C5C9T1; -.
DR EnsemblBacteria; ACS30233; ACS30233; Mlut_07010.
DR KEGG; mlu:Mlut_07010; -.
DR PATRIC; fig|465515.4.peg.664; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_1_11; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000738; 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..930
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000202780"
FT DOMAIN 422..596
FT /note="tr-type G"
FT REGION 51..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..438
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 456..460
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 481..484
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 535..538
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 571..573
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 113..140
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..251
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 431..438
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 481..485
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 535..538
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 930 AA; 97153 MW; B368998A8EF50279 CRC64;
MAKVRVHELA KELGITSKEA LSTLKDLGEF VSSASSTIEP PVVKKLRSAY PGAGKSAAKP
GSTPAAPAAG RSAAPKPAAA PSPRAVAPTS DAGAPAPGPA AGRTAATKPG VAPTPGPAAP
TPAAQVPAEP KAPQPSATPG SAAPKPGAAA PKPGAPRPGN NPFSPKGGSA GSRPGARPGG
RGGAPRPGNN PFAPSQGMRS GREDRAPRPG GPRPPAGAGG PRPGGPRPAA GAGGPRPGGP
RPNPGMMPKQ ITPAPQPARG RGRPGGGPGG GPGRPGGPGG RGGRGNAQGA FGRGGGPRKG
RKSKRAKRQE FEQQHTREIG GVKVPKGDGT TVLRLRRGAS LADFAEKIRA DVADLVKVLF
TLGEMASANQ SLDEETFQLL GDELGYKVQI VSPEDEDKEL LEAFDIDLEA EEANEDEADL
EPRPAVVTVM GHVDHGKTRL LDAIRSSNVI EGEAGGITQH IGAYQVPVEH EGEQRRLTFI
DTPGHEAFTA MRARGAKVTD IAVLVVAADD GVMPQTVEAL NHAQSAGVPI VVAVNKIDKD
TAAPDKIRGQ LTEYGLVPEE YGGDTMFVDV SARNNINIDQ LLEAILLTAD AALELTANPH
KAARGVAIEA NLDKGRGAVV TVLVQTGTLR VGDTMVVGSA HGRVRAMFDE NGNAVEAADP
SRPVQVLGLS SVPRAGDSFL VTDDERTARQ IAERREAADR NAQLAKRRKR ITLEDFDQAV
AEGKLDTLNL IIKGDASGAV EALEDSLLKI EVGEDEVQLR VIHRGVGAIT QNDVNLATVD
NAIIIGFNVR PAERVADLAD REGVDMRFYN VIYDAIDDIE NALKGMLKPE YEEVELGSAE
VREVFRSSKW GNIAGSLVRS GLIRRNAQAR LVRDGVVVSE HLRIESLRRF KEDATEVREG
YECGIGLGSF NDIKEGDVIE TFEMQEKPRV
