IF2_PSE14
ID IF2_PSE14 Reviewed; 843 AA.
AC Q48E77;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=PSPPH_4189;
OS Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
OS (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=264730;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1448A / Race 6;
RX PubMed=16159782; DOI=10.1128/jb.187.18.6488-6498.2005;
RA Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M.,
RA Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J.,
RA Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., Halpin R.,
RA Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M.,
RA Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A.,
RA Buell R.;
RT "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola
RT 1448A reveals divergence among pathovars in genes involved in virulence and
RT transposition.";
RL J. Bacteriol. 187:6488-6498(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; CP000058; AAZ34884.1; -; Genomic_DNA.
DR RefSeq; WP_011169449.1; NC_005773.3.
DR AlphaFoldDB; Q48E77; -.
DR SMR; Q48E77; -.
DR STRING; 264730.PSPPH_4189; -.
DR PRIDE; Q48E77; -.
DR EnsemblBacteria; AAZ34884; AAZ34884; PSPPH_4189.
DR KEGG; psp:PSPPH_4189; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_1_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000551; 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; 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.
FT CHAIN 1..843
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228231"
FT DOMAIN 343..512
FT /note="tr-type G"
FT REGION 94..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..359
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 377..381
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 398..401
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 452..455
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 488..490
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 94..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 352..359
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 398..402
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 452..455
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 843 AA; 90796 MW; 2D3A63A172E56117 CRC64;
MTQVTVKELA KVVDTPVERL LQQMREAGLP HTAAEQVVTD NEKQALLTHL KSGHKAKVEE
PRKITLQRKT TSTLRVAGSK SISVEVRKKK VFVQRSPEEI EAERKREMDE RRAVENAARQ
KAEEEAKRRA EEDARNQPAA GQPASAPAQP VAAAEPVREA PAPAAAAPAP ASAAPSADAR
KRDEQRRPDK PRADDRNARG GDGERKNAPH RASVKEKAPA PRVAPRTTDE ESDSFRRGGR
GKSRLKKRNA HGFQSPTGPV IRDVAIGETI TVGELSAQMS VKAAEVIKFM FKMGTPVTIN
QVLDQETAQL IAEELGHKVT LVSDNALEDS LAESLKFEGE SFSRAPVVTV MGHVDHGKTS
LLDYIRRAKV AAGEAGGITQ HIGAYHVETE RGMVTFLDTP GHAAFTAMRA RGAKATDIVI
LVVAADDGVM PQTIEAVQHA VAAGVPLVVA VNKIDKPGAD LDRIRSELSV HGVTSEEWGG
DTPFVSVSAK MGTGVDELLE AVLLQAEVLE LKATPSAPGR GVVVESRLDK GRGPVATVLV
QDGTLRQGDM VLVGSNFGRI RAMLDENGKP VKEAGPSIPV EILGLDGTPD AGDEMSVLAD
EKKAREVALF RQGKFREVKL ARAHAGKLEN IFENMGQEEK KTLNIVLKSD VRGSLEALQG
ALGGLGNDEV QVRVVGGGVG GITESDANLA LASNAVLFGF NVRADAGARK IVEQEGLDMR
YYNVIYDIIE DVKKALTGML GSDVRENILG IAEVRDVFRS PKFGAIAGCM VLEGTVYRNR
PIRVLREDIV IFEGELESLR RFKDDAAEVR AGMECGIGVK SYNDVKVGDK IEVFEKVQVA
RSL