IF2_SALRD
ID IF2_SALRD Reviewed; 1029 AA.
AC Q2S1N7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SRU_1777;
OS Salinibacter ruber (strain DSM 13855 / M31).
OC Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC Rhodothermaceae; Salinibacter.
OX NCBI_TaxID=309807;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13855 / CECT 5946 / M31;
RX PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H.,
RA Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA Legault B., Rodriguez-Valera F.;
RT "The genome of Salinibacter ruber: convergence and gene exchange among
RT hyperhalophilic bacteria and archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(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; CP000159; ABC44821.1; -; Genomic_DNA.
DR RefSeq; WP_011404519.1; NC_007677.1.
DR RefSeq; YP_445894.1; NC_007677.1.
DR AlphaFoldDB; Q2S1N7; -.
DR SMR; Q2S1N7; -.
DR STRING; 309807.SRU_1777; -.
DR PRIDE; Q2S1N7; -.
DR EnsemblBacteria; ABC44821; ABC44821; SRU_1777.
DR KEGG; sru:SRU_1777; -.
DR PATRIC; fig|309807.25.peg.1845; -.
DR eggNOG; COG0532; Bacteria.
DR eggNOG; COG3064; Bacteria.
DR HOGENOM; CLU_006301_0_1_10; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000008674; 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 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.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..1029
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335509"
FT DOMAIN 524..696
FT /note="tr-type G"
FT REGION 73..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..540
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 558..562
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 582..585
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 636..639
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 672..674
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 73..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..116
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..258
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..321
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..433
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 533..540
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 582..586
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 636..639
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1029 AA; 112063 MW; AD7D20A51B1132FA CRC64;
MATKTKDFQE KKLFQVVREL NVSEDRVVEF LEEEGYEEAL SGSGLNAKIV DEEAYLVLRE
EYADDAEVAA RIRELRSEED DGGPERDEVA TLDEEQAAEP ESATETAEEA AEPAVADDEE
EPRASGDAAP EAAPAEEDTS DATAPADAEA EPSGDEASAE ASADDAPADE APTDEAETAP
VDAADKDAAA IADEQKQAAQ EPDAEADASG QDTGEETSDT DAATEADATD DAEAESAAPE
PTEAEPETPA DETEAEDVSA DKETASAEEA DDHASDEHAP DEDAEAPEEP TEAEGEADDT
TEEETPAEGA DDAADDEADE EGETLKAGRY RLKGPSVVGK MDSDQLQRPD RKRKRKDKDK
DKDKSSKKDK KDKSNKKSKS KGKKQKGGGG GGPDEEDIEQ TLQETLQELE QGASRERQRR
RRRRRKRHEE ERQRRRERKR EQENILEVTE FVTTGELANL IGEPVSDVID TLFDAGMMVS
INQRLDTETI EFVADEYGYE VEFVAERDTQ AVEVEEDDPE DLEPRAPVVT VMGHVDHGKT
SLLDYVRNAN VVAGEEGGIT QHVGAHYVEL TDHDNEAIAF LDTPGHEAFT AMRARGAKAT
DIVILVVAAD DSVMPRTKEA INHAQAADVP IVVAINKMDK READAEKVRA ELADQNVLVE
EYGGDVQSAE VSAKTGDGIN ELLDKVLLQS EIMELKANPN REASGVIIES RLEKGRGNVI
TVLVQNGTLE TGDPFLAGIH SGSVRAMFNE RDNRIESVGP SQPALVLGCD GSPEVGDQFV
VMDSEGEARD VAQERQRIHR EQELRRQSQV SLDQVSRQMA EGEFHELNLI IKADVGGSVE
ALSDALLKLK TDEVAVNVIH SGVGAITESD VMLARASDAI ILGFQVRPTS GAREASQREE
VDIRTYSVIY AAIEDVRDAL EGLLSPERRE ETKGRAEVRD TFSVPDVGMV AGCYVNEGTV
GRNQKVRLVR DGVVQYEGEI SSLKRFEEDV SEVQSGYECG LSIENFDDLK VGDELETYVI
VEEARELEV
