IF2_STRMU
ID IF2_STRMU Reviewed; 916 AA.
AC Q8DVP9;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SMU_421;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AE014133; AAN58175.1; -; Genomic_DNA.
DR RefSeq; NP_720869.1; NC_004350.2.
DR RefSeq; WP_002262600.1; NC_004350.2.
DR AlphaFoldDB; Q8DVP9; -.
DR SMR; Q8DVP9; -.
DR STRING; 210007.SMU_421; -.
DR PRIDE; Q8DVP9; -.
DR EnsemblBacteria; AAN58175; AAN58175; SMU_421.
DR KEGG; smu:SMU_421; -.
DR PATRIC; fig|210007.7.peg.371; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_0_9; -.
DR OMA; NRDNRTG; -.
DR PhylomeDB; Q8DVP9; -.
DR Proteomes; UP000002512; 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; Reference proteome.
FT CHAIN 1..916
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137262"
FT DOMAIN 418..585
FT /note="tr-type G"
FT REGION 55..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..434
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 452..456
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 473..476
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 527..530
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 563..565
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 95..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 427..434
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 473..477
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 527..530
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 916 AA; 101538 MW; F03E349D19877CA3 CRC64;
MSKKRLYEIA KEIGKESKEI VEKAKSLGLE VKSHASSVEE SDAKRIVESF TVSVEPKAVT
PTSKVEKEAK AQEGSVAAEP KAAATKPAGR PRPQNRNFKA EREARAKAEA ERRQNNGERR
NQNKGQNNRQ KDNRNHGSQD RRNDNRNNRN RQNDNRRDNR NHFQNRQEAS KSQPTGPRFD
FKARAAALKA EQNAEYSRQS ETRFHEAQEA KRQAAQAKEK AKKLNQKEQP TVEAAATAAP
QAQPQTVEQV THPAAVDTRR KKQARPDKSR DFSHENEDGP KQNKHKKNRN KQNQVRNQKN
SNWNKKNKKS KNNRNHNANL KPVTERKFHE LPKEFEYTEG MTVAEIAKRI KREPAEIVKK
LFMMGVMATQ NQSLDADTIE LLMVDYGIEA HQKVEVDTAD IERFFVEDDY LNPKNMVERA
PVVTIMGHVD HGKTTLLDTL RNSRIATGEA GGITQHIGAY QIEEGGKKIT FLDTPGHAAF
TSMRARGASV TDITILIVAA DDGVMPQTIE AINHSKAADV PIIVAINKID KPGANPERVI
GELAEYGVIS TAWGGDSEFV EISAKFGQNI EELLETVLLV AEIQELKADP TVRAIGTVIE
ARLDKGKGAV ATLLVQQGTL HVQDPIVVGN TFGRVRAMTN DLGRRVKVAA PSTPVSITGL
NEAPMAGDHF AVYEDEKAAR AAGEERAKRA LLKQRQLTHR VSLDNLFDTL KAGEVKSVNV
IIKADVQGSV EALAASLLKI DVEGVKVNVV HSAVGAINES DITLAEASNA VIIGFNVRPT
PQARQQAEAD EVEIRLHSII YKVIEEVEDA MKGMLDPEFE EKIIGEALIR ETFKVSKVGT
IGGFMVTNGK ITRDSSARVI RDGVVVFDGK LASLKHYKDD VKEVGNGQEG GLMIENYNDI
KIDDTIEAYI MEEIKR
