IF2_FUSNN
ID IF2_FUSNN Reviewed; 737 AA.
AC Q8R5Z1;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=FN2020;
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX NCBI_TaxID=190304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355;
RX PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(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; AE009951; AAL94110.1; -; Genomic_DNA.
DR RefSeq; NP_602811.1; NC_003454.1.
DR AlphaFoldDB; Q8R5Z1; -.
DR SMR; Q8R5Z1; -.
DR STRING; 190304.FN2020; -.
DR PRIDE; Q8R5Z1; -.
DR EnsemblBacteria; AAL94110; AAL94110; FN2020.
DR KEGG; fnu:FN2020; -.
DR PATRIC; fig|190304.8.peg.488; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_0; -.
DR InParanoid; Q8R5Z1; -.
DR OMA; NRDNRTG; -.
DR BioCyc; FNUC190304:G1FZS-507-MON; -.
DR Proteomes; UP000002521; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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..737
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137204"
FT DOMAIN 237..404
FT /note="tr-type G"
FT REGION 69..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..253
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 271..275
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 292..295
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 346..349
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 382..384
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 69..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 246..253
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 292..296
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 346..349
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 737 AA; 81758 MW; 556823D7EE33F053 CRC64;
MKVRVHELAK KYEIKNKEFL EILKKDIGIT VTSHLSNLDE DQVNKIDDYF AKMNMLKVET
VEPVKVHKEK KEEKPIRKIM DEDENDEGEG YSQKNNKKAK FQQTKNKKNN NITFEEDGNS
HKNKGKKKKG RRTDFILKTV EATPDVVEED GIKIIKFRGE LTLGDFAEKL GVNSAEIIKK
LFLKGQMLTI NSPITLSMAE DLAADYDVLI EEEQEVELDF GEKFDLEIED KAADLKERPP
VITIMGHVDH GKTSLLDAIR TTNVVGGEAG GITQKIGAYQ VERDGKRITF IDTPGHEAFT
DMRARGAQVT DIAILVVAAD DGVMPQTVEA ISHAKVAKVP IIVAVNKIDK PEANPMKVKQ
ELMEHGLVSA EWGGDVEFVE VSAKQKINLD GLLDTILITA EILELKGNNK KRAKGVVLES
RLDPKIGPIA DILVQEGTLK IGDVIVAGEV QGKVKALLND KGERVNNATV SQPVEVIGFN
NVPDAGDTMY VIQNEQHAKR IVEEVRKERK IQETTKKTIS LESLSDQFKH EDLKELNLIL
RADSKGSVDA LRDSLLKLSN DEVAVSIIQA ASGAITESDV KLAEAAGAII IGYNVRPTTK
ALKEAEVSKV EIRTSGIIYH ITEDIEKALA GMLEPEYREE YLGRIEIKKV FKVSKVGNIA
GCIVIDGKVK NDSNIRILRD NVVIYEGKLA SLKRFKDDAK EVVAGQECGL GVENFNDIKD
GDVVEAFEMV EVKRTLK
