IF2_PSEA6
ID IF2_PSEA6 Reviewed; 869 AA.
AC Q15V72;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Patl_1695;
OS Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=342610;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6c / ATCC BAA-1087;
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., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Karls A.C.,
RA Bartlett D., Higgins B.P., Richardson P.;
RT "Complete sequence of Pseudoalteromonas atlantica T6c.";
RL Submitted (JUN-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; CP000388; ABG40216.1; -; Genomic_DNA.
DR RefSeq; WP_011574521.1; NC_008228.1.
DR AlphaFoldDB; Q15V72; -.
DR SMR; Q15V72; -.
DR STRING; 342610.Patl_1695; -.
DR EnsemblBacteria; ABG40216; ABG40216; Patl_1695.
DR KEGG; pat:Patl_1695; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001981; 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..869
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008301"
FT DOMAIN 369..542
FT /note="tr-type G"
FT REGION 51..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..385
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 403..407
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 424..427
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 478..481
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 514..516
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 63..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 378..385
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 424..428
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 478..481
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 869 AA; 94943 MW; 56CC30E6F3167011 CRC64;
MAEVSIEKLA ADIGTSVDRL VKQFKDADIV KAANENVTED EKRQLLDYLS KQHGGTGSEA
PKRMTLQRKT TSTLNMGKSK AVTVEVRKKR TYVKRTDVEE ARLAEEETAR ALAEQQAQLE
AEKAAAEEAK KAAEEKAKKA AESKAKAEAE RLARAEKAKK EAEARQAEES ALSPEEKAEQ
ERVRTEAENI RKKQEQESQR KLEEDAKKAA DEARKLAEEN SRRWKEEEER RKKQEAEEVH
VHSNRYAQEA EDADDIKIER GGRRRKKSKR NAGSDLKHAF NKPAQPVERI VRLGETITVS
DLASKLAIKA TEVIKAMMKM GEMATINQVL DQETAVLVVE EMGHKYELVN DNALEDELLA
DKISSELASR APVVTIMGHV DHGKTSLLDY IRRAKVAAGE AGGITQHIGA YSVETDNGRI
AFLDTPGHAA FTAMRARGAT ATDIVILVVA ADDGVMPQTK EAVQHSKAAG VPLIVAVNKM
DKESADPDRV KTELSQLEVI SEEWGGEHQF VNVSAKTGEG IDALLEAISL QAELLDLKAP
PTGSAKGIVI ESRLDKGRGP VASVLVQEGQ LKAGDILLCG IEYGRVRAMR DENGKDVAIA
GPSTPVEVLG LSGVPVAGED ALVVQDERKA REVATKRNAK QREIKLAKQQ KAKLENMFAN
MEAGDVSELN IVLKADVQGS VEAISDSLTK LSTSEVKVNI VGSGVGGITE TDASLAAASS
AIVVGFNVRA DASARRVIEA EEIDLRYYSV IYSLIDEVKM AMTGMLAPEF KQEIIGLAEV
RDVFKSPKLG AIAGCMVVEG TIKRSNPIRV LRENVVIYEG ELESLRRFKD DVQEVRNGVE
CGIGVKNYND VKVGDQIEVF EIVQVEREL
