IF2_JANMA
ID IF2_JANMA Reviewed; 937 AA.
AC A6T0Y8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=mma_2495;
OS Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=375286;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marseille;
RX PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D.,
RA Drancourt M.;
RT "Genome analysis of Minibacterium massiliensis highlights the convergent
RT evolution of water-living bacteria.";
RL PLoS Genet. 3:1454-1463(2007).
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; CP000269; ABR89281.1; -; Genomic_DNA.
DR RefSeq; WP_012080348.1; NC_009659.1.
DR AlphaFoldDB; A6T0Y8; -.
DR SMR; A6T0Y8; -.
DR STRING; 375286.mma_2495; -.
DR PRIDE; A6T0Y8; -.
DR EnsemblBacteria; ABR89281; ABR89281; mma_2495.
DR KEGG; mms:mma_2495; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR BioCyc; JSP375286:MMA_RS12945-MON; -.
DR Proteomes; UP000006388; 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; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR013575; IF2_assoc_dom_bac.
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; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 2.
DR SUPFAM; SSF46955; SSF46955; 1.
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..937
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008255"
FT DOMAIN 437..606
FT /note="tr-type G"
FT REGION 157..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..346
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 492..495
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 546..549
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 582..584
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 157..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..346
FT /note="Basic and acidic 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 492..496
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 546..549
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 937 AA; 100981 MW; 3DD8CD481EF68804 CRC64;
MASNNVAQFA TELKMPADVL LTQLRDAGVE KSSTSDELSK ADKDKLLDHL RRAHGVAPDG
EKKKITLTRK ETTEIKQADA TGKSRTIQVE VRKKRTFVKR DESTPEEAPV KAAAPVIDEA
EIERRAEEAR RQAELIARQE ADLREKQERL AKLEAEKEAQ AKALKQAEQA EAEAQKADAA
KPVEAKADES AQEEKKRVAA EESKKKAAQL AKDAAKEASE KAVATEAARK AVADEVAQIK
AMMNAPRRAI KAPEPAAPVA AKPAEGTLHK PADKKAGEKK DEKKPAVTAD KKSIKSANVS
STWQDDAKKR GAGIKTRGNT GGGRDGWRAG PKGRRPSHHD DRESNFQAPT EAVVKDVHVP
ETITVAELAH KMSVKASEVI KHLMKLGQMC TINQVLDQET AMILVEEMGH TAHAAKLDDP
EALLEQGEEH ADIEALPRAP VVTVMGHVDH GKTSLLDYIR RAKVASGEAG GITQHIGAYH
VETPRGMITF LDTPGHEAFT AMRARGAKAT DIVILVVAAD DGVMPQTKEA IAHAKAAGVP
LVVAINKIDK PGANMDRVKQ ELIAEQVVPE EYGGDSPFVP VSAKTGEGID ALLEQVLLQA
EVLELKAPVD APARGLVVEA KLDKGRGPVA TILVQSGTLK RGDVVLAGSA YGRVRAMLDE
NGKSITEAGP SIPVEIQGLT EVPNAGEEVM VMADERKARE IGLFRQGKFR DVKLAKQQAA
KLENMFENMG EGEVKNLPMI IKTDVQGSQE ALVGSLQKLS TSEVRVQVVH AAVGGISESD
VNLAVASKAV IIGFNTRADA SARKLAEANG VDIRYYNIIY DAVDEIKAAM SGMLAPEKRE
QALGLVEIRQ VILVSKVGAI AGCYVLEGVA KRGSSVRLLR DNVVVWTGEL DSLKRFKDDV
KEVKAGFECG LTLKNFNDIK EGDQLEVFEV QEIARTL
