IF2_PELPB
ID IF2_PELPB Reviewed; 986 AA.
AC B4SCE7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Ppha_0398;
OS Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Pelodictyon.
OX NCBI_TaxID=324925;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5477 / BU-1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of Pelodictyon phaeoclathratiforme BU-1.";
RL Submitted (JUN-2008) 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; CP001110; ACF42727.1; -; Genomic_DNA.
DR RefSeq; WP_012507222.1; NC_011060.1.
DR AlphaFoldDB; B4SCE7; -.
DR SMR; B4SCE7; -.
DR STRING; 324925.Ppha_0398; -.
DR EnsemblBacteria; ACF42727; ACF42727; Ppha_0398.
DR KEGG; pph:Ppha_0398; -.
DR eggNOG; COG0532; Bacteria.
DR eggNOG; COG3170; Bacteria.
DR HOGENOM; CLU_006301_0_1_10; -.
DR OMA; KPGANTE; -.
DR OrthoDB; 79988at2; -.
DR Proteomes; UP000002724; 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.
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..986
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000117334"
FT DOMAIN 483..653
FT /note="tr-type G"
FT REGION 75..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..499
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 517..521
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 539..542
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 593..596
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 629..631
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 75..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 492..499
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 539..543
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 593..596
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 986 AA; 109121 MW; 6DDE7886360E840E CRC64;
MALEDMEKKY RISDIARELQ VSPQEVLLFV KQEGGRVAST SSMVGEEIHG LIFGHFSVEK
KMVDETKKIR AEKEKRLSRL EEQSRKTYEK EQHLSETLSP PAPPLVVVHE PKKEVIVAAP
IENIPEPPSK PLEIPVAETP ASEEPDAPPA VTELIEQPVV IEQQPLAPVS DAPVPPVIIE
LPVPSEVPES QVLPESRVLP ESQVLSESPL LPEPPVLSEP QEQQELPELP ELPEIPALPE
PAPKKEEPSV NEHLVSFDAP QMMGGLTVLG TLDMQAGRHK KNRKKNFQEQ ADALKDEFEP
KPAEESRVEE KVVVAKKPPV KAAADVKPKP VVADSSSSAK KKGKKKKKPA VDDKVISANI
QKTISGIDDR SSTGSRQKFR KMRRNERERE HEEDEAFREA QRLVVRVTEY ASPHELAELM
GITAKDIIQK CFALGKFVTI NQRLDKESIE LIALEFGFEA EFISEVEATA VIVTEDAEAD
MQTRPPVVTI MGHVDHGKTS LLDYIRNSKV VAGESGGITQ HIGAYEVTVE GDRKITFLDT
PGHEAFTAMR ARGAQVTDIV ILVVAADDSV MPQTIEAINH AKAAGVPIVV ALNKIDKVEA
NPEKIKTQLS EAGVLVEEWG GVYQCQEISA KKGIGIAELM EKVLTEAEMR ELRGNYSREV
PASGIIVESE LDKGKGVIST VLVQRGILKV GDPFVAGNTM GKVRALMDER GKRIPFANPS
QPVRVLGFED LPQSGDALTV MVTDREARDL AQKRQVIRRE HDFRRSTRVK LDSIARQIKE
GLMKELSVII KADTDGSIQA LADGLMKIQN EEVKVQIIHQ GVGQITETDV LLAAASDAII
IGFRVRPNVN AKKLAEKEDL DVRFYSVIYH VLEDVEKALE GMLSPELHEE SLGSLEIRQI
FKVPKIGNVG GCYMLEGKMF RDSKVRLLRD GVQIYEGQLA ALKRFKDDVK EVDAGYECGM
SLKNYDDIKV GDIVEAYKIV EKKRKL
