IF2_HALHL
ID IF2_HALHL Reviewed; 890 AA.
AC A1WXV1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Hhal_1749;
OS Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira
OS halophila (strain DSM 244 / SL1)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Halorhodospira.
OX NCBI_TaxID=349124;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 244 / SL1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hoff W.,
RA Richardson P.;
RT "Complete sequence of Halorhodospira halophila SL1.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000544; ABM62513.1; -; Genomic_DNA.
DR RefSeq; WP_011814535.1; NC_008789.1.
DR AlphaFoldDB; A1WXV1; -.
DR SMR; A1WXV1; -.
DR STRING; 349124.Hhal_1749; -.
DR PRIDE; A1WXV1; -.
DR EnsemblBacteria; ABM62513; ABM62513; Hhal_1749.
DR KEGG; hha:Hhal_1749; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_1_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000647; 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..890
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008251"
FT DOMAIN 390..559
FT /note="tr-type G"
FT REGION 50..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..406
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 424..428
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 445..448
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 499..502
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 535..537
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 53..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 399..406
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 445..449
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 499..502
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 890 AA; 97162 MW; 01838AC3901896CB CRC64;
MAETTVKEFA QTVGIPVERL QAQLEAAGLG RRDDGAALSA EDKATLLAHL RQGSPEQEEE
GGGSDGSPKK ITLKRRSHSQ LKMPAGRDAG SRGPRQTRTV NVEVRKRRTY VKRSDIEAEE
KRKQEEAEEA AAQLERALEQ EEAKREEDAA EAQRAGDTAV TGGDEAEQAP SEEAAPAEEA
EPSAADAEAV EESGVEVQAA EPEETAADET ARAQAEALKE KPKSQQDEAK KREEERERKR
AELEAKRERE AEERAQRKQE AKPKKKKAEQ PAGGRGAGAR RGGKKRGGGT AAKQLQQEFE
RPTAPVVREV EIPETITVAE LADRMSVKAA ALIKEMMKQG VMATINQAID QETAAILVEE
MGHKPKLQRD DDVEEELLRQ GEQPEGEQIG RAPVVTVMGH VDHGKTSLLD YIRRAKVASG
EAGGITQHIG AYRVEGENGS ATFLDTPGHQ AFTAMRARGA QMTDIVVLVV AADDGVMPQT
KEAVEHARAA EVPIVVAVNK MDKEDADPNR VKQELSQMEV IPEEWGGDVQ FVHVSAMTGE
GMDELIEAIV LQAELQELKA VKDCPARGVV LESSLDKGRG PVATVLVQNG YLHRGDTVIS
GTEFGRVRAL VDEHGKRVNE AGPSTPVEVL GLSGLPDAGD DIMVVEDERK AREVAESRSE
RQREKRLAQQ QAARMENLFS QMKEDEVSTI NLLVKADVHG SAEALRQSLE DLSHEEVRVR
VVSSGVGAIT ESDVNLALAS EAIMIGFNVR ADAAAKRMVQ EHGVDLHYYS VIYDAIEQVK
NAISGMLEPT LEEHILGTAE VREVFRSSKL GQVAGCLVVD GVVRRRNPIR VLRDSVVIYE
GELESLRRFK DDVNEVRAGT ECGIGVKNYN DVRAGDQIEC YERVEVQRSL
