IF2_MARN8
ID IF2_MARN8 Reviewed; 848 AA.
AC A1U600;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Maqu_3348;
OS Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter
OS aquaeolei).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Marinobacteraceae; Marinobacter.
OX NCBI_TaxID=351348;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700491 / DSM 11845 / VT8;
RX PubMed=21335390; DOI=10.1128/aem.01866-10;
RA Singer E., Webb E.A., Nelson W.C., Heidelberg J.F., Ivanova N., Pati A.,
RA Edwards K.J.;
RT "Genomic potential of Marinobacter aquaeolei, a biogeochemical
RT 'opportunitroph'.";
RL Appl. Environ. Microbiol. 77:2763-2771(2011).
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; CP000514; ABM20419.1; -; Genomic_DNA.
DR RefSeq; WP_011786760.1; NC_008740.1.
DR AlphaFoldDB; A1U600; -.
DR SMR; A1U600; -.
DR STRING; 351348.Maqu_3348; -.
DR EnsemblBacteria; ABM20419; ABM20419; Maqu_3348.
DR KEGG; maq:Maqu_3348; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_1_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000998; 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; 1.
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.
FT CHAIN 1..848
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008267"
FT DOMAIN 344..511
FT /note="tr-type G"
FT REGION 90..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..360
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 378..382
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 399..402
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 453..456
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 489..491
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 174..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 353..360
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 399..403
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 453..456
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 848 AA; 92213 MW; D8F7D04C7785896A CRC64;
MAEVTVKQLA ADVGAPVDRL LKQIVEAGLK ARSENDAVTS DEKQQLLAYL RKNHGEAEAE
PRKITLKRKT TTTLKAGKAK TVNVEVRKRR TYIKRAELQP EPEAEAPAPE EPVQAPAAEQ
APVEEAPKVA AEAAPAEAPE TEAPAAAETE AKAAPEPAAE SAEPAIAPED IPMPPPEDEG
RDRKPKKKKE KVRERGDDIE EGKPKKKQAG HRGPRSRPVE EPVVLSEDEE ETTLRKPLRA
KKKPKEKRHA FERPTKPMVR EVQIPETITV GDLAQRMAVK SADVIKTLMG MGVMATINQA
LDQETAILVT EELGHKPKAV SEDAFEEEVL SEITGPDEGK EKIKRAPVVS VMGHVDHGKT
SLLDHIRRAK VAAGESGGIT QHIGAYHVET EHGMVSFLDT PGHAAFTAMR ARGAQCTDIV
ILVVAADDGV MPQTKEAVEH ARSAGVPIVV AINKMDKEEA DPDRIKNELS ALEVIPEDWG
GDVQFVPVSA HTGMGIDDLL EAVLLQAEIL ELEASPDAAA KGVVVESSLE RGRGSVATVL
VQNGTLRQGD MVVAGSFFGK VRAMTDEAGR QVKEAGPSIP VEILGLNGTP DAGDEFFAVA
DEKKAKELAE FRQTREREQR LQRQQAAKLE NMFENMGKDE VKTLNVVLKT DVRGSLEAIT
KALQDLGNDE VQVKIVSSGV GGIAETDVSL AMATNAVIFG FNVRADTASK RLVEQEGLDL
RYYSIIYNLI DDVKAALTGM LKPEFREDIV GIADVRDVFR SPKFGQVAGC MVTEGTVYRN
KPIRVLRDNV VIFEGELESL RRFKDDVAEV RNGMECGIGV KGYDVKVGDQ IEVFDRVRVE
RQLESTGA
