ID IF2_RENSM Reviewed; 956 AA.
AC A9WPV8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, 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};
GN OrderedLocusNames=RSal33209_0656;
OS Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 /
OS NBRC 15589 / NCIMB 2235).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Renibacterium.
OX NCBI_TaxID=288705;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235;
RX PubMed=18723615; DOI=10.1128/jb.00721-08;
RA Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S.,
RA Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT reductive evolution away from an environmental Arthrobacter ancestor.";
RL J. Bacteriol. 190:6970-6982(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; CP000910; ABY22403.1; -; Genomic_DNA.
DR AlphaFoldDB; A9WPV8; -.
DR SMR; A9WPV8; -.
DR STRING; 288705.RSal33209_0656; -.
DR KEGG; rsa:RSal33209_0656; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_1_11; -.
DR Proteomes; UP000002007; 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; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 1.10.10.2480; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 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 NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 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; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
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..956
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335502"
FT DOMAIN 449..620
FT /note="tr-type G"
FT REGION 68..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..465
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 483..487
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 508..511
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 562..565
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 598..600
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 458..465
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 508..512
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 562..565
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 956 AA; 98746 MW; B71C39AB05E014D5 CRC64;
MPDSVRAETG ESVAKARVHE LAKELGITSK DAVAKLQELG EFVRSASSTI EAPVVKKLRD
AFPDAVAAPE AAAPKAPARP APKAPAKPAE AQASVKPVET QAPATPAAAK AAATPVAPAA
PAVKEQKEGS AARPGAGGPR PGNNPFATSQ GMPRAGARAE GERPAAAPAS GAGRPRPGGP
RPGAPRPGNN PFASSQGMPR SGGRGDGERS GGPRPAAGSG GPRPAAGSGG PRPAAGSGGP
RPGAGSGASR PGGGGGNRPT PGMMPNRTER PAPAGRGAGG GAGGPGRGGG ARPGGGAPAG
GGFGKGGRGR GGTQGAFGKG GAGRGKQRKS KRAKRQELEQ MSAPSLGGVS VPRGDGNTVV
RLRRGSSITD FADKIEANPA ALVTVLFHLG EMATATQSLD EETFALLGEE LGYKLQVVSP
EDEERELLST FDIDFDAELE AEGDEDLQAR PPVVTVMGHV DHGKTRLLDA IRNSDVVAGE
HGGITQHIGA YQVNHVHEGE VRKITFIDTP GHEAFTAMRA RGAKVTDIAI LVVAADDGVM
PQTVEALNHA QAAGVPIVVA VNKIDKEGAN PEKIRGQLTE YGLVPEEYGG ETMFVDVSAR
QNQNIDALLE AVMLTADAAL DLRANPNKDA RGIAIEANLD KGRGSVATVL VQSGTLAVGD
TIVAGTAHGR VRAMFDDDGT AVTEAGPSRP VQVLGLSSVP RAGDTFFVTG DERTARQIAE
KREAADRNAA LAKRRKRISL EDFDQAVADG KVDTLNLILK GDVSGAVEAL EDSLLKIDVG
EGVQLRVIHR GVGAITQNDV NLATVDSAII IGFNVKPAER VAELADREGV DMRFYSVIYA
AIDDIELALK GMLKPEYEEV QLGTAEIREI FRSSKFGNIA GSIVRSGLIR RNAKARVLRA
GVLIGDNLTV DSLKRVKDDA TEVREGFECG IGLGSFNDLQ LEDIIETFEM REKPRV
//
