IF2_PHEZH
ID IF2_PHEZH Reviewed; 994 AA.
AC B4RC55;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=PHZ_c3439;
OS Phenylobacterium zucineum (strain HLK1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Phenylobacterium.
OX NCBI_TaxID=450851;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLK1;
RX PubMed=18700039; DOI=10.1186/1471-2164-9-386;
RA Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.;
RT "Complete genome of Phenylobacterium zucineum - a novel facultative
RT intracellular bacterium isolated from human erythroleukemia cell line
RT K562.";
RL BMC Genomics 9:386-386(2008).
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; CP000747; ACG79848.1; -; Genomic_DNA.
DR RefSeq; WP_012523986.1; NC_011144.1.
DR AlphaFoldDB; B4RC55; -.
DR SMR; B4RC55; -.
DR STRING; 450851.PHZ_c3439; -.
DR PRIDE; B4RC55; -.
DR EnsemblBacteria; ACG79848; ACG79848; PHZ_c3439.
DR KEGG; pzu:PHZ_c3439; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_1_5; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001868; 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; 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; 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..994
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093809"
FT DOMAIN 492..662
FT /note="tr-type G"
FT REGION 1..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..508
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 526..530
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 548..551
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 602..605
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 638..640
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 24..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..161
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..195
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 501..508
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 548..552
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 602..605
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 994 AA; 105815 MW; BFF08BA5E51D902F CRC64;
MSDENNNGRN SAPGGRQPLT LKPRAAGSVS SGTVKQSFSH GRTKTVVVET KRARTHAPAG
GNLAAPSAAE RRVFEPQKPA GPAQAPRAPQ GAGDGLSAEE RAARQRAIEL ARQQEADRRA
REERARAEAE AARAAQQKAA QAAAEPPAAP PPAPAAPPAA AAPAAPAAEA APAPKPAPSP
RPVPPSAPAP QAARPAAEAP PRQAGAGQTR TYQPSPDRRD DRPSTTTYRP ERPSNRFDTS
TFNQRAPRRD DDRGPRPPRR DDDRGPRRDD RPQGARPEGG GTVRYSALAP RPAPGGPRGP
GGPRGPGGPR IGAAAPPATP EIQRAARQAP RPGMGVDRRP DEDDRRRDPG KAISRAKGAP
NRREGRLTIQ AVAGDADGAE RMRSLASVRR AREREREKRK GGAQEQARVA REVVIPDVIT
VGELANRMAT RGVEVIKFLM RQGVMLKIND VIDNDTAELV ATEFGHTVKR VSEADVEEGF
IGAEDVDDHL LPRPPVVAVM GHVDHGKTSL LDALRSTDVV SGEHGGITQH IGAYQVRLAD
GQRVTFLDTP GHAAFSAMRM RGANVTDIVI LVVAADDGVM PQTVEAIQHA KAAGAPIIVA
INKIDKPDAD PTRVINELLQ HEIVVESLGG ETQAVEVSAT QKMGLDDLIE NILLQAEVLD
LKANPDRTAD GSVIEAKLDK GRGAVATVLV KRGTLKRGDI VVAGSSWGRV RALLNERGEQ
LQEATPSTPV EILGLDGTPD PGEPFAVVEN EARARELTEY RQRVKREKAG APVASASLAD
MMAKLADKKV SELPVIIKAD VQGSAEAIVG SLDKLATDEV RARIILSGAG AINESDVLLA
KGAGAPILGF NVRASKQARD LAEREGVEIR YYAIIYDLID DIKGVLSGML APIQRETFLG
NAEVLQAFDI TKVGRVAGCR VTEGVVRKGA RVRIVREDVV ILELGVLKTL KRFKDEVNEV
QAGQECGMAF EGFQDIKAGD VIECFNLEEV KRSL
