IF2_PHOLL
ID IF2_PHOLL Reviewed; 909 AA.
AC Q7MYY7;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=plu4529;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
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; BX571874; CAE16901.1; -; Genomic_DNA.
DR RefSeq; WP_011148605.1; NC_005126.1.
DR AlphaFoldDB; Q7MYY7; -.
DR SMR; Q7MYY7; -.
DR STRING; 243265.plu4529; -.
DR EnsemblBacteria; CAE16901; CAE16901; plu4529.
DR GeneID; 24169317; -.
DR KEGG; plu:plu4529; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR BioCyc; PLUM243265:PLU_RS22355-MON; -.
DR Proteomes; UP000002514; 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; 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 PANTHER; PTHR43381; PTHR43381; 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; 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..909
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137231"
FT DOMAIN 408..577
FT /note="tr-type G"
FT REGION 49..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..424
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 442..446
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 463..466
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 517..520
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 553..555
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 84..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 417..424
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 463..467
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 517..520
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 909 AA; 99903 MW; DC3D46CFAC6FF3D8 CRC64;
MTDVTVKSLA EEIQTSVDRL VQQFADAGIK KTETDFVSQK EKEALLAHLN REQGGSAGKP
DKLTLQRKTR STLNVSGTDG KSKPVAVEVR KKRTYVNRDA VEQAKAEEQA KREAEEQARR
EAEEKAQREA EAAAKKLVEE QAKREAEEKA KREAAEKAKR QAAESEKVTN QHTEHKQKPA
QTDKTIQSEK ARREAEAADL KRKAEEEMRR KVEEEAKRVA EEARRMAEEN QDKWSSDSDS
IDSDDYHVTT SRHARAAEDE NDAKVEGDRR ARGRSGKATR QKKNNKHSES KADREEARAV
GRTKGKQRKT STLQQSFNKP VAAVNRDVVI GETITVAELA NKMAVKGSQV IKAMMKMGAM
ATINQVIDQE TAQLVAEEMG HKVILRRENE LEEALMSDRD TGEAVAEPRA PVVTIMGHVD
HGKTSLLDYI RSTKVASGEA GGITQHIGAY HVETDSGMIT FLDTPGHAAF TSMRARGAKA
TDIVVLVVAA DDGVMPQTIE AIQHAKAASV PVVVAVNKID KPEADPDRVK SELSQHGVQP
EEWGGETQFI NVSAKAGIGI DELLDAILLQ AEVLELKAVR SGMASGVVIE SFLDKGRGPV
ATVLVQEGTL NKGDIVLCGF EYGRVRAMRD ELGREVFSAG PSIPVEILGL SNVPAAGDEA
TVVRDEKKAR EVALYRQGKF REVKLARQQK SKLENMFANM EEGEVSELNI VLKSDVQGSC
EAIREALEQL STDEVKVKII GSGVGGITET DATLAAASNA IILGFNVRAD ASARRVVENE
SLDLRYYSVI YSLIDEVKQA MSGMLAPEYK QQIMGLAEVR DVFKSPKFGA IAGCMVTEGT
IKRNNPIRVL RDNVVIYEGE LESLRRFKDD VNEVRNGMEC GIGVKNYNDV RVGDMIEVFE
IIEVKRSIA
