IF2_PORG3
ID IF2_PORG3 Reviewed; 979 AA.
AC B2RHM9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=PGN_0355;
OS Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS 12257 / NCTC 11834 / 2561).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=431947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
RX PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA Nakayama K.;
RT "Determination of the genome sequence of Porphyromonas gingivalis strain
RT ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT rearrangements in P. gingivalis.";
RL DNA Res. 15:215-225(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; AP009380; BAG32874.1; -; Genomic_DNA.
DR RefSeq; WP_012457447.1; NZ_CP025930.1.
DR AlphaFoldDB; B2RHM9; -.
DR SMR; B2RHM9; -.
DR STRING; 431947.PGN_0355; -.
DR EnsemblBacteria; BAG32874; BAG32874; PGN_0355.
DR GeneID; 29255597; -.
DR KEGG; pgn:PGN_0355; -.
DR eggNOG; COG0532; Bacteria.
DR eggNOG; COG3266; Bacteria.
DR HOGENOM; CLU_006301_0_0_10; -.
DR OMA; VIFAMNK; -.
DR BioCyc; PGIN431947:G1G2V-391-MON; -.
DR Proteomes; UP000008842; 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.
FT CHAIN 1..979
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093811"
FT DOMAIN 478..646
FT /note="tr-type G"
FT REGION 67..392
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 305..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; 107544 MW; DF4C5B7FF8F45DDB 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
RNAGGGNHPS 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
