ID IF2_ALTMD Reviewed; 868 AA.
AC B4RXT8; F2GAC8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN OrderedLocusNames=MADE_1008920;
OS Alteromonas mediterranea (strain DSM 17117 / CIP 110805 / LMG 28347 / Deep
OS ecotype).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=1774373;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17117 / CIP 110805 / LMG 28347 / Deep ecotype;
RX PubMed=18670397; DOI=10.1038/ismej.2008.74;
RA Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S.,
RA Johnson J., Friedman R., Rodriguez-Valera F.;
RT "Comparative genomics of two ecotypes of the marine planktonic copiotroph
RT Alteromonas macleodii suggests alternative lifestyles associated with
RT different kinds of particulate organic matter.";
RL ISME J. 2:1194-1212(2008).
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; CP001103; AEA97922.1; -; Genomic_DNA.
DR RefSeq; WP_012518253.1; NC_011138.3.
DR AlphaFoldDB; B4RXT8; -.
DR SMR; B4RXT8; -.
DR GeneID; 56342192; -.
DR KEGG; amc:MADE_1008920; -.
DR HOGENOM; CLU_006301_6_3_6; -.
DR Proteomes; UP000001870; 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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.56.50; Putative DNA-binding domain, N-terminal subdomain of bacterial translation initiation factor IF2; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR004161; EFTu-like_2.
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 NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 2.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46955; Putative DNA-binding domain; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
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.
FT CHAIN 1..868
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093755"
FT DOMAIN 368..537
FT /note="tr-type G"
FT REGION 49..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..384
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 402..406
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 423..426
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 477..480
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 513..515
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 92..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 377..384
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 423..427
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 477..480
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 868 AA; 95580 MW; 32AA374822B8D3FD CRC64;
MADVSIEKLA SDIGTTVDRL VGQFKDAGIS KSAGEQVNED EKQKLLDHLS KQHGSAAEPT
RMTLKRKTTS TLSVGKSKEV KVEVRKKRTY VKRSDIEEQQ RQAEEEAKRL EEEARLKREA
EEKAAAEAKK AAEEKARKAQ EAKKAAEEER VRRAEQAKKE AEARKKDEPE LTEAEKAEAE
AARQEEERLR KAQEEEAQKK LEEDAKKAAD EARKLAEENE RRWKEEEERR KKAEAEEVHL
HSNRYAQEAE DEEDMQVERS SRRRRKSKKN AGEHLKQGFN KPAAPVERVV KLGATITVGE
LASKLAIKSN EVIKTMMKMG EMATINQVLD QDTAVLVIEE MGHKYELVND NALEDELLAD
GTDGEKTSRA PVVTIMGHVD HGKTSLLDYI RRAKVADGEA GGITQHIGAY KVQTDNGEIT
FLDTPGHAAF TAMRARGATA TDIVILVVAA DDGVMPQTKE AVQHARAAGV PLIVAVNKMD
KETADPDRVK TELSQLEVIS EEWGGEHQFC NVSAKTGMGV DELLEAIVLQ SELLDLQAVA
EGPGRGIVIE SRLDKGRGPV ASVLVQEGQL RAGDILLCGE EYGRVRAMRD ENGKDMKLAG
PSTPVEVLGL SGVPVAGEDA AVVKDERKAR EVAAKRHQKK RELKLARQQK AKLENMFANM
ESGDVSELNI VLKADVQGSV EAISESLIKL STSEVKVNIV GSGVGGITET DATLAAASGA
IVLGFNVRAD ATARRVLEAE EIDLRYYSVI YNLIDEVKAA MSGMLAPEFK QEIIGLAEVR
DVFKSPKLGA IAGCMVTEGN VKRSNPIRVL RDNVVIYEGE LESLRRFKDD VQDVRNGMEC
GIGVKNYNDV KVGDQIEVFE IVEVKREI
//
