IF2_STRMK
ID IF2_STRMK Reviewed; 881 AA.
AC B2FN90;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Smlt3389;
OS Stenotrophomonas maltophilia (strain K279a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=522373;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K279a;
RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA Parkhill J., Thomson N.R., Avison M.B.;
RT "The complete genome, comparative and functional analysis of
RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT resistance determinants.";
RL Genome Biol. 9:R74.1-R74.13(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; AM743169; CAQ46817.1; -; Genomic_DNA.
DR RefSeq; WP_012480878.1; NC_010943.1.
DR AlphaFoldDB; B2FN90; -.
DR SMR; B2FN90; -.
DR STRING; 522373.Smlt3389; -.
DR EnsemblBacteria; CAQ46817; CAQ46817; Smlt3389.
DR KEGG; sml:Smlt3389; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_2_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000008840; 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; 1.
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..881
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093830"
FT DOMAIN 380..549
FT /note="tr-type G"
FT REGION 53..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..396
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 414..418
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 435..438
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 489..492
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 525..527
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 53..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..218
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 389..396
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 435..439
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 489..492
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 881 AA; 94768 MW; DBB93B53D9B4F3A5 CRC64;
MSQQTTIRKL AELVNTPVEK LLEQLAGAGM KFSGPDQVVT SSEKVKLLGF LRRSHGKPEQ
APEESDQSAK KITLNRRKQQ EVTVNSGRSK TTVNVEVRQK RTYVKDGARA MTPDEERADI
LRKLEESRAR NLAEQQALAE KDRLRDEAIV RAREEEIAAK ERAEAEKKAA EEAAAAAKAA
EALAAAKPKR APIDETAPRP PRTPAAAPAA PRSAPPPPRN DDRNNRSAPR NERGPGDRFA
GQMHLSAADR ARRGNSNNSN TRGRPGGRNQ AGGRRDMSRG GNNAGPHAFE RPTAPVVREV
AIGDTITVAD LAQKLALKGG EVVKALFKMG VMATITQSID HDTAALVTEE LGHKAIRAND
NDAEDALLAS TGENQGEATQ RPPVVTIMGH VDHGKTSLLD YIRRTKVATG EAGGITQHIG
AYHVDTPKGV ISFLDTPGHA AFTSMRARGA KLTDIVVLVV AADDGVMPQT KEAIQHARSA
GVPLIVAINK IDKSDADPMR VKNELLSEQV VAEDFGGDTQ MVEISAKTGL GIDDLLDAIS
IQAELLELKA VDEGRASGVV IESSLDKGRG PVATVLVQQG RLKKGDYLVC GIQYGRVRAL
FDETGKQPEF AGPSIPVQVL GLSGVPEAGD DFVVVEDERL AKDVAQQRET KRRESRLVAT
AGSRMEDIMA TLGKGEGQQV LNLVIKADVQ GSVQALSQAL VALSNEDIRI NVIHSGVGGI
TESDANSAAA SKATVIGFNV RADASARRII ESNGVDLRYF SIIYDVIDQV KQVASGLLGV
EIREEIIGIA EVRDVFRSSK LGAVAGSMVI EGVVRRNKPI RVLRDSVVIF EGELESLRRF
KENVEEVRNG TECGIAVKAY NDVKPGDQIE CFERIEVPRT L
