IF2_PORGI
ID IF2_PORGI Reviewed; 979 AA.
AC Q7MXE4;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=PG_0255;
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83;
RX PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA Fraser C.M.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE015924; AAQ65478.1; -; Genomic_DNA.
DR RefSeq; WP_005874178.1; NC_002950.2.
DR AlphaFoldDB; Q7MXE4; -.
DR SMR; Q7MXE4; -.
DR STRING; 242619.PG_0255; -.
DR EnsemblBacteria; AAQ65478; AAQ65478; PG_0255.
DR KEGG; pgi:PG_0255; -.
DR PATRIC; fig|242619.8.peg.235; -.
DR eggNOG; COG0532; Bacteria.
DR eggNOG; COG3266; Bacteria.
DR HOGENOM; CLU_006301_0_0_10; -.
DR OMA; VIFAMNK; -.
DR OrthoDB; 347113at2; -.
DR BioCyc; PGIN242619:G1G02-240-MON; -.
DR Proteomes; UP000000588; 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..979
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137232"
FT DOMAIN 478..646
FT /note="tr-type G"
FT REGION 67..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..494
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 512..516
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 534..537
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 588..591
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 624..626
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 106..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 487..494
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 534..538
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 588..591
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 979 AA; 107534 MW; 1CE8345E29FB6D6F CRC64;
MSIKLFSLAK ELNVGVGSLA GFLRKKGFDV EDNNPNVRIE NEEFDLLLTE FGKSLPKGEA
ERIRKKFVKQ KQGTPASAPS AKEETAGMAA KEAQVIATEV PQDMRPRFTI KGKVETEKPA
EPVPSPKDKE PDTVREDKPA RETAPVKEET KVVPVKEDKP KEEKPKQEEP KREEPKPEEP
VQAAPVAKPV EKPVDKPQQP VMTQKPQEAE TPPPAQEMEK KEDTEEVFRL KTNTQEPQVK
VVGKIDLSSI NSSTRPKKKT KEDRQREQND ADGKKKRKRI NKAAVDVKKE AAKVSGEQGK
RNAGGGNHSS GNKNNNRPAQ QQSNASGGRK NNKRQSLPPK VEISDEDVQR QVKETLARLT
TKKTSTTLGR GAKYRKDKRD AASRAAQDAM ELNSEEQHTL KLTEFVTVSD LSNMMDVPVN
EVIATCMSIG MMVGINQRLD AETINIVAEE FGFKTEFVSA DLVEAIAPEE DNEEDLVARP
PIVTVMGHVD HGKTSLLDRI RNTNVIEGEA GGITQHIGAY GLKLPSGRRI TFLDTPGHEA
FTAMRARGAK ITDIAIIIVA ADDDVMPQTV EAINHASAAG VPMVFAINKI DKPAANPERI
KEQLANMNYL VEDWGGKYQS QEISAKKGIN ITELLEKVLL EADILELKAN PNRRAIGSII
ESSLDKGRGY VSTVMVQNGT LNMGDVVLAG TCHGRIKAMF NERNQRVKQA GPSEPVLILG
LNGAPAAGDT FNVLETEQEA REIANRREQL QREQGLRTHK ILTLEDISRR RAIGNFQELN
LIVKGDVDGS VEALSDSLIR LSTEEIQVNV IHKAVGQISE SDVVLAAASS AIIIGFQVRP
SVAARKQAET DGVEIRTYSI IYDTIEDIKS AMEGMLSPEI REEVTGSLEV LQTFKISKVG
TIAGCMVKEG KVKRTSKVRL IRDGIVIHTG ELGSLKRFKD DAKEVVAGLE CGLNLAHSND
IQDGDIIEAF DEIEIKKTL
