IF2_SPHAL
ID IF2_SPHAL Reviewed; 845 AA.
AC Q1GVI9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Sala_0612;
OS Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256)
OS (Sphingomonas alaskensis).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=317655;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13593 / LMG 18877 / RB2256;
RX PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA Robb F.T., Kjelleberg S., Cavicchioli R.;
RT "The genomic basis of trophic strategy in marine bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
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; CP000356; ABF52333.1; -; Genomic_DNA.
DR RefSeq; WP_011540923.1; NC_008048.1.
DR AlphaFoldDB; Q1GVI9; -.
DR SMR; Q1GVI9; -.
DR STRING; 317655.Sala_0612; -.
DR PRIDE; Q1GVI9; -.
DR EnsemblBacteria; ABF52333; ABF52333; Sala_0612.
DR KEGG; sal:Sala_0612; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_1_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000006578; 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; 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; 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.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..845
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008343"
FT DOMAIN 344..514
FT /note="tr-type G"
FT REGION 1..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..360
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 378..382
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 400..403
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 454..457
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 490..492
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 97..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 353..360
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 400..404
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 454..457
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 845 AA; 91056 MW; 340597DE8B9450BD CRC64;
MSDEQDKPTL SRKPLGLKRT VEAGQVQQQF SHGRRNTVVV EVKRRRVLGR PGEAAPTPEV
EEAKAAPAPA PAPAAPRPAA PKPAAVDSLM TRQERQAQLL REAEEARMAA LEENRRREEA
ERARAAEEER ARAEKREEQA ATKAPEPAPT PAASAPDATA ADAPPAAEGP VETAARPATA
SAAPAPRRFT PVEALKRPEP KRPEPKASRG GENRRQSGKL TVTRALNEDE GARARSLAAL
KRAREKEKRS HMTSSGPREK QVREVVVPDT ITVQELANRM AEKGADLVKA LFKMGMPVTV
NQTIDQDTAE LLVTEFGHEI KRVSEADIDI RHDEDVDDAA QLKPRAPVVT IMGHVDHGKT
SLLDALRGAN VQAGEAGGIT QHIGAYQVKA KDGSVITFLD TPGHEAFTEM RQRGANVTDI
VILVVAADDG LKPQSIEAIN HAKAAGVPII VAINKVDKEG ANPQRVRERL LEHELVVEEM
GGDVQNVEVS ALKKTGLDKL LDAIALQAEI MELKANPDRA AEGTVIEAKL DKGRGPVATI
LVRRGTLKVG DIFVCGAESG RVRALVDDHG KQVKQATPSM PVEVLGLGGV PMAGDTLIVV
ENEARAREVA AYRQEQALKK RTAQAPVSLE GMFSALADKA NVIEYPVVIK GDVQGSVEAI
VNALNKLSTD EIRVRVLHAG AGAITESDVT LAASTRAPII GFNVRPNAKA REIANREKVR
FLYYDVIYHL TADVAKEMAG ELGPERIENV VGRAEVKDVF PAGKRDKAAG LLVLEGSIRK
GLHARLTRDD VIVSATTIAS LRRFKDDVAE VRAGLECGVV LADTNDIKPG DHLEVFEVEL
RERTL
