IF2_STREM
ID IF2_STREM Reviewed; 947 AA.
AC B4U1E8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Sez_0443;
OS Streptococcus equi subsp. zooepidemicus (strain MGCS10565).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=552526;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGCS10565;
RX PubMed=18716664; DOI=10.1371/journal.pone.0003026;
RA Beres S.B., Sesso R., Pinto S.W.L., Hoe N.P., Porcella S.F., Deleo F.R.,
RA Musser J.M.;
RT "Genome sequence of a lancefield group C Streptococcus zooepidemicus strain
RT causing epidemic nephritis: new information about an old disease.";
RL PLoS ONE 3:E3026-E3026(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; CP001129; ACG61815.1; -; Genomic_DNA.
DR RefSeq; WP_012515091.1; NC_011134.1.
DR AlphaFoldDB; B4U1E8; -.
DR SMR; B4U1E8; -.
DR EnsemblBacteria; ACG61815; ACG61815; Sez_0443.
DR KEGG; sez:Sez_0443; -.
DR HOGENOM; CLU_006301_5_0_9; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000001873; 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..947
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093827"
FT DOMAIN 448..617
FT /note="tr-type G"
FT REGION 55..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..464
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 482..486
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 503..506
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 557..560
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 593..595
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 81..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 457..464
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 503..507
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 557..560
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 947 AA; 103969 MW; E221716BF976A3CF CRC64;
MSKKRLHEIA KEIGKSSKEV VERAKSLGLD VKSHASSVEE ADANKIASSF AAGVTKDAQA
GSAKDKQVAE QKAKAAKATT PQPAAATQEA SQPVAVKPKS RNFKAEREAR AKEQAARRQA
GQNRSNDRKS DYRQLGRSQG QQTERAGHKS QNQQRDRRFD NRPSSGNNRN DGHRQAGNRD
KNRSFNANSR QQDTGRQGQT QAGAPKIDFK ARAAALKAEQ NAEYARQRES RFREQEEAKR
LEQQARQEAK AAALKAQTED KKHREASAKA TEPIASMAAA PVAKPVDKRR KKQNRPDKGH
DRDHGLEDGQ KKNKKSWNSQ NQVRNQKNSN WNNNKKNKKG KHHKNSNTAP KPVTERKFHE
LPKEFEYSEG MTVAEIAKRI KREPAEIVKK LFMMGVMATQ NQSLDGDTIE LLMVDYGIEA
KAKVEVDEAD IERFFTDDSY LNPENIVERA PVVTIMGHVD HGKTTLLDTL RNSRVATGEA
GGITQHIGAY QIEEAGKKIT FLDTPGHAAF TSMRARGASV TDITILIVAA DDGVMPQTIE
AINHSKAAGV PIIVAINKID KPGANPERVI SELAEHGIIS TAWGGECEFV EISAKFNKNI
DELLETVLLV AEVEELKADP TVRAIGTVIE ARLDKGKGAV ATLLVQQGTL HVQDPIVVGN
TFGRVRAMTN DLGRRVKSAE PSTPVSITGL NETPMAGDHF AVYADEKAAR AAGEERAKRA
LLKQRQNTQR VSLDNLFDTL KAGEIKTVNV IIKADVQGSV EALAASLLKI DVEGVRVNVV
HSAVGAINES DVTLAEASNA VIIGFNVRPT PQARQQADAD DVEIRLHSII YKVIEEVEEA
MKGKLDPEYQ EKVLGEAIIR ETFKVSKVGT IGGFMVVNGK VTRDSSVRVI RDSVVIFDGK
LASLKHYKDD VKEIGNAQEG GLMIEGFNDI KVDDTIEAYV MEEIIRK
