IF2_LEGPL
ID IF2_LEGPL Reviewed; 868 AA.
AC Q5WT36;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=lpl2689;
OS Legionella pneumophila (strain Lens).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=297245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lens;
RX PubMed=15467720; DOI=10.1038/ng1447;
RA Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA Glaser P., Buchrieser C.;
RT "Evidence in the Legionella pneumophila genome for exploitation of host
RT cell functions and high genome plasticity.";
RL Nat. Genet. 36:1165-1173(2004).
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; CR628337; CAH16930.1; -; Genomic_DNA.
DR RefSeq; WP_011216621.1; NC_006369.1.
DR AlphaFoldDB; Q5WT36; -.
DR SMR; Q5WT36; -.
DR EnsemblBacteria; CAH16930; CAH16930; lpl2689.
DR KEGG; lpf:lpl2689; -.
DR LegioList; lpl2689; -.
DR HOGENOM; CLU_006301_6_1_6; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000002517; 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.
FT CHAIN 1..868
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228208"
FT DOMAIN 368..537
FT /note="tr-type G"
FT REGION 158..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..384
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 402..406
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 423..426
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 477..480
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 513..515
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 158..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 377..384
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 423..427
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 477..480
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 868 AA; 94619 MW; 5B8621F897B1F424 CRC64;
MADVTVKQLA QVVGIPVERL LNQLQEAGLS FTDDQQTVNE EQKRILLNHL KGSSNRDISA
APERITLRRK SMSQVTVGHD MHSGKTVNIE VRKKKTFIKR SAIPEQAEVE EPVVPPVVEE
PAHEEITVVS EVSADTSELK ETEEHPVIEP VAALDETVKE EEKINSEENT AESQDELTHA
NTDVIENLVD VVEEAIPVSK KEEVKPEKVS KKKHLEQTDS DISEFKKGKK KPKYHTFEHD
EEEQELHRRG GRSKFKKKKG TEKSDKYREA EETLTHGFAL PTAPIVREVL IPETITVAEL
AKRMSVKAAE VIKVMMSLGA MATINQVIDQ ETSVIVVEEM GHKPVIIKED AVETGLGEAI
SKGTKTEGRA PVVTIMGHVD HGKTSLLDYI RRTKVAAGEA GGITQHIGAY HVSTPKGDIT
FLDTPGHAAF TAMRARGAQA TDIVILIVAA DDGVKPQTIE AIQHAKAAKV PIIVAINKMD
KPDADPERVM NELSVQEVIP EAWGGDTMFV NISAKSGMGI DDLLDAILLQ SEVLELKAVT
DGAAKGVVIE SRLDKGRGPV ATVLVQSGTL HKGDILLAGF QYGRVRALVS DNGDLVDSAG
PSIPVEVLGL SAIPHAGDEA VVVPDEKKAR EVALFRQGRF RDVKLARRQK TTIEGIMENM
TATESKVLNI VLKADVQGSL EAISDALTKL STDEVKVEVI SSGVGGITES DVHLAIASNA
ILIGFNVRAD GTAKRLAEQE SVSIHYYSVI YDIVDQIKGA LTGMLAPQFK EEIVGIAEVR
DVFKSPKIGA IAGCMVIEGV VKRNNPIRVL RSNVVIYEGT LESLRRFKDD VLEVRQGFEC
GIGVKNYNDV KPGDLIEVFE TVEIKRDL
