IF2_NITMU
ID IF2_NITMU Reviewed; 876 AA.
AC Q2Y7W2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Nmul_A1864;
OS Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosospira.
OX NCBI_TaxID=323848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25196 / NCIMB 11849 / C 71;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC
RT 25196.";
RL Submitted (AUG-2005) 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; CP000103; ABB75159.1; -; Genomic_DNA.
DR RefSeq; WP_011381179.1; NZ_FNVK01000004.1.
DR AlphaFoldDB; Q2Y7W2; -.
DR SMR; Q2Y7W2; -.
DR STRING; 323848.Nmul_A1864; -.
DR PRIDE; Q2Y7W2; -.
DR EnsemblBacteria; ABB75159; ABB75159; Nmul_A1864.
DR KEGG; nmu:Nmul_A1864; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002718; 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; IPR009061; DNA-bd_dom_put_sf.
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; 2.
DR SUPFAM; SSF46955; SSF46955; 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..876
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335492"
FT DOMAIN 378..547
FT /note="tr-type G"
FT REGION 164..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..394
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 412..416
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 433..436
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 487..490
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 523..525
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 168..182
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 387..394
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 433..437
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 487..490
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 876 AA; 95075 MW; 78162F6F5F19035C CRC64;
MSQMNVEQFA SELGVLPTVL LEQLQAAGVR KHMTEDSLTE KDKTQLLEYL RKIHGAKEEK
GRISLPRRQT SEIKKADSTG KPRSIQVEVR KKRVFVKGVD LPVERKTAEI PAPAAPSVPP
VRTPVIDAAQ QALRQEEARR QAELIARQAA ELREKRLRER PPVVEIKEPE EPAPPFVPAA
PVAGPEAVPV APETPSAAPG ETVAAVEAEA APSQPASTEG TLHKPAVKPE EKADKKKKPA
KQVVWKEEKV EKRGLKTRGD LSGAKGGWRA RKDKHGRTEE PAPHAFSAPT EPVVHEVLVP
ETISVGALAQ KMSIKAAEVI KALMKMGNMV TINQMLDQET AMIVVEELGH VAKYAALDSP
ESFLADTEIA PSELKMEARA PVVTVMGHVD HGKTSLLDYI RRTRVASGEA GGITQHIGAY
HVETERGMVT FLDTPGHEAF TAMRARGAKV TDLVILVVAA DDGVMPQTVE AIHHAKAGKV
PIVVAMTKID KPEANPERIR QELVTQEVVP EDWGGETMFV EVSAKTGQGI DDLLESVLLQ
AEVLELKAPK DAPAKGIVIE SRLDKGRGPV ATMLVQSGTL KRGDILLAGA AYGRVRAMLD
ESGKQVEQAG PSIPVEIQGL SEVPVAGESV VALTDERKAR EIALFRQGKF RDVKLAKQQA
AKLENVFEQR GEVKVLSLII KADVQGSYEA LTHALQQLST DEVKVNIIHS GVGAITESDI
NLALASKAVV IGFNSRADAV ARKLINSAGV DVRYYSIIYE AVDEIKAALS GMMAPERKEN
ITGLLEIREV FRISKVGAVA GCLVQEGFVR RGSLVRVIRN GQVIHTGELD SLKRFKDDVK
EVRAGFECGL SLKNFNDIQV GDQLETYEIQ VIARTL
