IF2_PROMH
ID IF2_PROMH Reviewed; 916 AA.
AC B4F2B9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, 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}; OrderedLocusNames=PMI3418;
OS Proteus mirabilis (strain HI4320).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=529507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI4320;
RX PubMed=18375554; DOI=10.1128/jb.01981-07;
RA Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA Parkhill J., Mobley H.L.T.;
RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT both adherence and motility.";
RL J. Bacteriol. 190:4027-4037(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; AM942759; CAR46704.1; -; Genomic_DNA.
DR RefSeq; WP_004246237.1; NC_010554.1.
DR AlphaFoldDB; B4F2B9; -.
DR SMR; B4F2B9; -.
DR STRING; 529507.PMI3418; -.
DR PRIDE; B4F2B9; -.
DR EnsemblBacteria; CAR46704; CAR46704; PMI3418.
DR GeneID; 6802058; -.
DR KEGG; pmr:PMI3418; -.
DR eggNOG; COG0532; Bacteria.
DR eggNOG; COG3064; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000008319; 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; IPR004161; EFTu-like_2.
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; PF03144; GTP_EFTU_D2; 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..916
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093814"
FT DOMAIN 415..584
FT /note="tr-type G"
FT REGION 50..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..431
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 449..453
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 470..473
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 524..527
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 560..562
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 61..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 424..431
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 470..474
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 524..527
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 916 AA; 101072 MW; BB99709DDDC53BC2 CRC64;
MTDETVKSLA EEIQTPVERL VQQFADAGIK KTVSDSVSQK EKETLLAWLN RDKESTSQPE
KLTLQRKVRS TLSVPGTGGK NKSVAIEVRK KRTYVNRDAV EKAQAAEQAQ REAEEKARRE
AEEKAQREAQ EKAQREAEEK AKREAEEAKK KAEEKAKREA EEAKREAAEL AKREAAEKDK
VKQNEKPKAD KADQEKARRI AEQAELKRKT EEAQRRKAEE EARIAAEKAR RLAEENAEKW
TSDTSSETEG TDYHVTTSRY ARDAEDESDA EVEGGRGRGR AAKAPRPKKN NRHSEKADRE
EARAAGRSNK KGKGRKNSTL QQGFNKPAAA VNRDVVIGET ISVADLANKM AVKGSEVIKT
MMKMGAMATI NQVLDQETAQ LVAEEMGHKV ILRRENELEE QVMNDRDTSD EMAVSRAPVV
TIMGHVDHGK TSLLDYIRST KVASGEAGGI TQHIGAYHVK TDKGEITFLD TPGHAAFTSM
RARGAQVTDI VVLVVAADDG VMPQTIEAIQ HAKAANVPVV VAVNKIDKPE ADPDRVKTEL
SQYGILPEDW GGETQFIHVS AKQGLGIDEL LDAILLQAEV LELKAVKEGM ASGVVIESYL
DKGRGPVATI LVREGTLNKG DIVLCGFEYG RIRAMRNELG KEVQSAGPSM PVEILGLSNV
PSAGDEATVV RDEKKAREVA LYRQGKFREV KLARQQKSKL ENMFANMEEG KVSELNIVLK
TDVQGTCEAI TDALVKLSTD EVKLKIIGSG VGGITETDAT LAAASDAIIL GFNVRADASA
RRIIEQESVD LRYYSVIYSL IDEIKSAMSG MLEPEYKQEI MGLAEVRDVF KSPKFGAIAG
CMVVEGNIKR NNPIRVLRDN VVIYEGELES LRRFKDDVNE VRNGMECGIG VKNYNDVRVG
DMIEVFQVIE IKRSID
