IF2_KOCRD
ID IF2_KOCRD Reviewed; 967 AA.
AC B2GKR5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=KRH_16040;
OS Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Kocuria.
OX NCBI_TaxID=378753;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201;
RX PubMed=18408034; DOI=10.1128/jb.01853-07;
RA Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Complete genome sequence of the soil actinomycete Kocuria rhizophila.";
RL J. Bacteriol. 190:4139-4146(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; AP009152; BAG29951.1; -; Genomic_DNA.
DR RefSeq; WP_012398672.1; NC_010617.1.
DR AlphaFoldDB; B2GKR5; -.
DR SMR; B2GKR5; -.
DR STRING; 378753.KRH_16040; -.
DR EnsemblBacteria; BAG29951; BAG29951; KRH_16040.
DR KEGG; krh:KRH_16040; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_1_11; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000008838; 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; 2.
DR PRINTS; PR00315; ELONGATNFCT.
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..967
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093795"
FT DOMAIN 460..632
FT /note="tr-type G"
FT REGION 34..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..476
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 494..498
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 519..522
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 573..576
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 609..611
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 117..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 469..476
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 519..523
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 573..576
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 967 AA; 100648 MW; 92F334A6CAF5FF93 CRC64;
MAKPRVHELA KELGITSKEA ISKLQELGEF VRGASSTVEP PVAKKLRTAF PAGGDSAPAA
KPAAKAPAQG VKKPAAAGPK PGAKAPAKPA ASGNAARAEK PAASEAPKAA AASSEAPKSA
APQQGTAPAA ASESSAPGTP ASSAPRPGGA TPGPRKSPAP GAKPGQSAPR PGNNPFASQQ
GMGRSEGGAQ RGGPRPGGQQ RSGKPGAPRP GNNPFAAQQG MRSANSGQGG PRPGGPRPGG
PRPAQSGQGG PRPGAPRTGA PRQGQGGPRP GGPRPSPNMM PGQTTSVAPI GSRPAPGSGP
RRGGGPGGGP GGGGGFRGRG GRGGTQGAFG RGGARGKHRK SKRAKRQELE QMSAPAVGGV
SVPHGDGSTV VRLRRGASLM DFAEKINANP ASLVTVLIHL GEMATQTQSL DEETFQLLGA
ELGYQIQVVS PEDEERELLE SFDIDLDAEL EAEGEDVLAP RPPVVTVMGH VDHGKTRLLD
AIRNTKVIEG EAGGITQHIG AYQISTEVDG QERLITFIDT PGHEAFTAMR ARGAQVTDIA
VLVVAADDGV MPQTVEALNH AQAANVPIVV AVNKVDKPDA NPDKIRGQLT EYGLVPEEYG
GDTMFVDVSA RENLNIDELL DAIVLTADGA LELQATPDKN ARGVAIEANL DKGRGAVCTV
LVQSGTLKVG DSIVAGAAYG RVRAMFDEMG RTVEAATPSR PVQVLGLSTV PRAGDTFLAT
QEERTARQIA EKREAADRNA QLAKRRKRIT LESFDEAVAE GKIDTLNLII KGDVSGAVEA
LEDSLLKIDV GEEVQLRVIH RGVGAITQND VNLATVDNAV IIGFNVRPAE RVTELADREG
VEMKFYSVIY NAIDEVESAL KGMLKPEYEE VELGTAEIRE VFRSSKWGNI AGAYVTKGLI
RRNGKARLVR DGNVVQDNLS IDSLRRFKDD ATEVREGYEC GIGLGSFNDI HEGDIIETWE
MREKPRD
