IF2_RHIWR
ID IF2_RHIWR Reviewed; 856 AA.
AC A5VCZ5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Swit_3816;
OS Rhizorhabdus wittichii (strain DSM 6014 / CCUG 31198 / JCM 15750 / NBRC
OS 105917 / EY 4224 / RW1) (Sphingomonas wittichii).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Rhizorhabdus.
OX NCBI_TaxID=392499;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6014 / CCUG 31198 / JCM 15750 / NBRC 105917 / EY 4224 / RW1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Halden R.U., Miller T.R., Salzberg S.L., Eisen J.A.,
RA Richardson P.;
RT "Complete sequence of chromosome of Sphingomonas wittichii RW1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000699; ABQ70161.1; -; Genomic_DNA.
DR RefSeq; WP_012050000.1; NC_009511.1.
DR AlphaFoldDB; A5VCZ5; -.
DR SMR; A5VCZ5; -.
DR STRING; 392499.Swit_3816; -.
DR PRIDE; A5VCZ5; -.
DR EnsemblBacteria; ABQ70161; ABQ70161; Swit_3816.
DR KEGG; swi:Swit_3816; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_1_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001989; 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; IPR013575; IF2_assoc_dom_bac.
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; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 1.
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..856
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008344"
FT DOMAIN 356..526
FT /note="tr-type G"
FT REGION 1..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..372
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 390..394
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 412..415
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 466..469
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 502..504
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 22..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..95
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 365..372
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 412..416
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 466..469
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 856 AA; 91944 MW; 31CE9D27F338207B CRC64;
MSDNDKPKLG MRAPLGLKRT VETGQVKQSF SHGRSNTVVV EVKRRRIVPG RPGEAEPQVT
EETAAAPVAP APAPAPAAQA PVAPRPAPAP IPTGRPMTPL ERREQQERLL REAEEARMAA
LEETRRREER AKAEATEEER RRAEENRRAE EEAERAAAAA AAAATAEAET AAAAPREEAP
AAAGTAEEAP RTSSSTMPPP RRFTPVPSPK RPEPPRPQQR DRKGDDRRQS GKLTVTRALD
DDSGARARSL AALKRAREKD KRAHQAGTVQ QKQVRDVAVP ETITVGELAN RMAERGADLV
KALFKMGMPV TVNQSIDQDT AELLVTEFGH NIKRVSDSDV DLITSDDVDA AETLQPRPPV
VTIMGHVDHG KTSLLDALRG TDVASGEAGG ITQHIGAYQV QVKSGAKITF LDTPGHEAFS
EMRARGANIT DIVVIVVAGD DGLRPQTIEA ISHTRAAGVP MIIAINKMDK PGSNAQRVRE
ALLQHDVQVE SMGGDVQEVE VSALKKTGLD ELIEKIELQA ELLELKANPD RPAEGTVVEA
TLDKGRGAVA TILVGRGTLK VGDIFVVGAE SGKVRALIDD KGRNIKEAGP SLPVEILGLS
GVPSAGDQLS VVENEARARE VAAYRAGVIH QKRTTAAPAS LESMFSALRE QKAQQYPVVV
KADAQGSVEA IVGSLNKIST DLIQVRILHA GVGGITESDV SLAAASKAPI IGFNVRANAK
AREIATRDGV ALKYYDVIYD LLDEIRAAMA GQLGPEYLEH VVGRAEIREV FSAGKHGKAA
GLLVLEGYIR QKLRARIMRD DVIIYNGSIS SLRRFKDDVP EVRAGLECGI TLEATTDIKP
GDIVETFEVE ERERTL
