IF2_PELUB
ID IF2_PELUB Reviewed; 734 AA.
AC Q4FNM9;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SAR11_0389;
OS Pelagibacter ubique (strain HTCC1062).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Pelagibacterales;
OC Pelagibacteraceae; Candidatus Pelagibacter.
OX NCBI_TaxID=335992;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC1062;
RX PubMed=16109880; DOI=10.1126/science.1114057;
RA Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L., Baptista D.,
RA Bibbs L., Eads J., Richardson T.H., Noordewier M., Rappe M.S., Short J.M.,
RA Carrington J.C., Mathur E.J.;
RT "Genome streamlining in a cosmopolitan oceanic bacterium.";
RL Science 309:1242-1245(2005).
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; CP000084; AAZ21210.1; -; Genomic_DNA.
DR RefSeq; WP_011281674.1; NC_007205.1.
DR AlphaFoldDB; Q4FNM9; -.
DR SMR; Q4FNM9; -.
DR STRING; 335992.SAR11_0389; -.
DR EnsemblBacteria; AAZ21210; AAZ21210; SAR11_0389.
DR GeneID; 66294886; -.
DR KEGG; pub:SAR11_0389; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002528; 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; 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; 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..734
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228222"
FT DOMAIN 238..405
FT /note="tr-type G"
FT REGION 39..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..254
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 272..276
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 293..296
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 347..350
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 383..385
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 45..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 247..254
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 293..297
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 347..350
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 734 AA; 79862 MW; D7530851BD5EF8E3 CRC64;
MENKKTKLTL SGIAKKSIEN IELAKTQSKN SVVIEKKPSK FAPRSSFTRP ASVRSKPAVS
TTSSFPPRTA SVPKPASPIT NDYEKRKLAE QRATRRLKGD TGKPETKKRE LKLTVSRALS
DEIEARSRSM ASLKRAKLKE NRELTKEEIQ ESLKPVKRDV NIPEAITVRE LSNRMAEQSS
NVIKHLFGMG VTVTINQTLA ADTAEYLVKE FGHNPIRETK AEEIIQKIKE SRSENLKNRP
PIVTVMGHVD HGKTSVLDVL RSANVVSGEF GGITQHIGAY QIQHESNKLT FIDTPGHAAF
TEMRARGSKL TDVVVLVVAA DDGVKPQTIE SIKHAKAANV PIVVAINKCD LPEADPQKIK
NQLLEYELIA EDLSGDTLMV EISAKNKKNL DKLVESIVLQ AEILDLKTDF ESKATGIVLE
SKIDIGRGAV ATVVVTSGTI KKGDFFVSGL KWGKVRALIN DKGENVNEAP PSMPVEILGI
NGAAKSGDDF IVLDSEKEAK TLSQNRAEES KTGGSPLTFA TQDSAFADKS AAELNIIVKS
DVHGSAEAIK SAINQITHDE VKPKIILSDI GMVTETDVTL AKASNAALIA FNVKPSKEAK
KLAENEKIVI SSYNIIYEVL DYIKLRMSGL LAPDVQEKII GTAQILEIFK VSGTGKVAGS
KVTEGEITSG ASARVVRDGA IIYTGKISTI FREKDQAKQV SNGQECGITL KDFIDFQKND
TIEAFSTTTT DRTV
