IF2_STAHJ
ID IF2_STAHJ Reviewed; 716 AA.
AC Q4L5X1;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SH1645;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(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; AP006716; BAE04954.1; -; Genomic_DNA.
DR RefSeq; WP_011275931.1; NC_007168.1.
DR AlphaFoldDB; Q4L5X1; -.
DR SMR; Q4L5X1; -.
DR STRING; 279808.SH1645; -.
DR EnsemblBacteria; BAE04954; BAE04954; SH1645.
DR GeneID; 58062165; -.
DR KEGG; sha:SH1645; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000543; 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 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..716
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228246"
FT DOMAIN 218..387
FT /note="tr-type G"
FT REGION 52..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..234
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 252..256
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 273..276
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 327..330
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 363..365
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 55..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 227..234
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 273..277
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 327..330
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 716 AA; 78731 MW; CE46042019045EBF CRC64;
MSKKRIYEYA KELNVKSKEI IDELKNMNVE VSNHMQALED DQIKTLDKKF RQQESNNNTK
QNTQNNHQKQ QNNNNNKNNN KQSNKGNANQ KGNNNNKNNA KNNKNNKNNK NNKNNKNNKG
NKNNKPAAEP KEMPSKITYE EGITVGELAD KLNIESSGII KKLFLLGIVA NINQALDEET
LELIADDYGV ELEKEVVVNE EDLSIYFDEE EADPDAIERP AVVTIMGHVD HGKTTLLDSI
RHTKVTAGEA GGITQHIGAY QIENAGKKIT FLDTPGHAAF TTMRARGAQV TDITILVVAA
DDGVMPQTIE AINHAKEANV PTIVAVNKID KPTANPDRVM QELTEYGLIP EDWGGETIFV
PLSALSGEGI DDLLEMIGLV AEVQELKANP DKQAVGTVIE AELDKSRGPA ASLLVQNGTL
NVGDSIVVGN TYGRIRAMVN DLGQRIKSAG PSTPVEITGI NDVPLAGDRF VIFKDEKQAR
RIGEARHEAS VIQQRQESKN VSLDNLFEQM KQGEMKDLNV IIKGDVQGSV EALAASLMKI
DVEGVNVRII HTAVGAINES DVTLANASNG IIIGFNVRPD AGAKRAAEAE NVDMRLHRVI
YNVIEEIESA MKGLLDPEFE EQVIGQAEVR QTFKVSKVGT IAGSYVTEGK ITRNAGVRII
RDGIVLFEGE LDTLKRFKDD AKEVAQGYEC GITIEKFNDI KEGDIIEAFE MVEIER
