IF2_LAWIP
ID IF2_LAWIP Reviewed; 961 AA.
AC Q1MQY8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, 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=LI0535;
OS Lawsonia intracellularis (strain PHE/MN1-00).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Lawsonia.
OX NCBI_TaxID=363253;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHE/MN1-00;
RA Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT "The complete genome sequence of Lawsonia intracellularis: the causative
RT agent of proliferative enteropathy.";
RL Submitted (NOV-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; AM180252; CAJ54589.1; -; Genomic_DNA.
DR RefSeq; WP_011526618.1; NC_008011.1.
DR AlphaFoldDB; Q1MQY8; -.
DR SMR; Q1MQY8; -.
DR STRING; 363253.LI0535; -.
DR KEGG; lip:LI0535; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_7; -.
DR OMA; VIFAMNK; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002430; 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; 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..961
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008263"
FT DOMAIN 460..627
FT /note="tr-type G"
FT REGION 146..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..476
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 494..498
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 515..518
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 569..572
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 605..607
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 160..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 469..476
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 515..519
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 569..572
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 961 AA; 106236 MW; 25050F6FC052AF0C CRC64;
MINDKIKVKD LAIELGVSTK DLLRVLRELE ISAKSTISNI SIEDLPKIRA QFNTPNTNKE
EERRQIQPGV ILRRKRQQPS TNQTDIKLNP VDTNVSESTI QTENLILENK NTLSPHIEET
TEKIPATTNE ILYNSQIAKI VQYPTPSVPN KTLTTTPHQT KKNHSEKDVL ESHDSSNKNI
KQSSSQNTEK TNRKPAASAI PEGSSAPSLL PPVSEQIRRL HDEETENSSS EEKNVDIQQK
EIPSTQVRVI SKPNITQSHS WDANNTRSSS GQRTETEKQS NTAPHTDSRE HTGHNKRPVS
YQGQNRNNFI ATPDTIPNVE HDGQNKKKRH TSRRSTEFNH KFQYNNEDDD ISRQNRGRKR
HKQKTTSQVT TQPIKLTKRK IRVEEAIRVA DMAHQMGLKA NEIIKVLFNL GVMATINMSL
DIDTATLVAA EFGYEVEKIG FTEEDYLVAT APEQSESLKR RPPVVTIMGH VDHGKTSLLD
AIRKTNVTGG EAGGITQHIG AYHVTTKSGE IVFLDTPGHE AFTTMRARGA QVTDIVVLVV
AADDGVMEQT REAVNHARAA NVPIMVAVNK MDKPEANPDR VLRELSDIGL VPEDWGGDTI
VTKVSAKSLD GIDELLELLA LQTDILELKA NPDKPARGHI VEAKLDKGRG PIATVLIQEG
TLHQGDTFVC GVFSGRVRAM FNDQGKKVKD AGPSMPIEVQ GFEGVPEAGE AFICLPDEKL
ARRIAESRAI KQREKELAKE SRVTLETFLS KTSNEKEAQV LNLVVKSDVQ GSLEAILEAL
RKLSTAKVRI NIIHGGSGAI TESDILLASA SDAIVIGFNV RPTAKVKEVA EQENVDIRFY
DIIYKLVEEI KSAMAGLLAP ISREVYLGQA DVREIFNVPK IGTIAGSHVS DGKVLRNAGV
RLLREGVVVY TGGIASLRRF KEDVREVQKG YECGISLENF NDIKLGDVIE SFETVEEAAS
L
