IF2_HELAH
ID IF2_HELAH Reviewed; 941 AA.
AC Q17WQ8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Hac_1159;
OS Helicobacter acinonychis (strain Sheeba).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=382638;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sheeba;
RX PubMed=16789826; DOI=10.1371/journal.pgen.0020120;
RA Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G.,
RA Gressmann H., Achtman M., Schuster S.C.;
RT "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a
RT host jump from early humans to large felines.";
RL PLoS Genet. 2:1097-1110(2006).
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; AM260522; CAJ99918.1; -; Genomic_DNA.
DR RefSeq; WP_011578025.1; NC_008229.1.
DR AlphaFoldDB; Q17WQ8; -.
DR SMR; Q17WQ8; -.
DR STRING; 382638.Hac_1159; -.
DR EnsemblBacteria; CAJ99918; CAJ99918; Hac_1159.
DR KEGG; hac:Hac_1159; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_4_1_7; -.
DR OMA; VIFAMNK; -.
DR OrthoDB; 347113at2; -.
DR BioCyc; HACI382638:HAC_RS04990-MON; -.
DR Proteomes; UP000000775; 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; 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..941
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008252"
FT DOMAIN 440..609
FT /note="tr-type G"
FT REGION 61..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..456
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 474..478
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 495..498
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 549..552
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 585..587
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 62..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 449..456
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 495..499
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 549..552
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 941 AA; 105210 MW; 50F08DB45471FFD1 CRC64;
MSGMVDLKEF LAELGKTQKE LKNVIEQAKD IGLELRTNSK MTPEEAEKLY KYIVDGIKEQ
IQSNRPIKKD KEGAATPKAS NKKTSKTPKK EEAKSQLKPK NTKKKKKEAP TPILKKKGIE
IVDTFENKTP PVENAPKVVT PSQSQIEKAK QKLQEIQKSR EALNKLTQSN TNNANNANSA
KKEISEVAKQ EREQEHLDNK RRENIKRYTG FRVIKRNDDE NETQNSVTEN KKPTQSAVAI
FEDIKKEWQE KDKETKKAKK SNKPKAIPAA KNNKSHKIDF SDARDFKGNN DIYDDETDEI
LLFDLHEQDN LNEEEEKEIR QNINDRARIQ RKNPWMNEGG IKRQSKKKRV FRNDNSQKVV
QSVISIPEEV CVYEFAQKAN LNLADVIKTL FNLGLMVTKN DFLDKDSIEI LAEEFHLEIS
VQNTLEEFEV EEVLEGVKKE RPPVVTIMGH VDHGKTSLLD KIRDKRVAHT EAGGITQHIG
AYMVEKNGKW VSFIDTPGHE AFSQMRNRGA QVTDIAVIVI AADDGVKQQT VEALEHAKVA
NVPVIFAMNK MDKPNVNLDK LKAECAELGY NPVDWGGEYE FIPISAKTGD GIDNLLETIL
IQADIMELKA IEEGRARAVV LEGSVEKGRG AVATVIVQSG TLSVGDSFFA ETAFGKVRTM
TDDQGKSIQN LKPSMVALIT GLSEVPPAGS VLIGVENDSI ARLQAQKRAT YLRQKALSKS
TKVSFDELSE MVANKELKNI PVVIKADTQG SLEAIKNSLL ELNNEEVAIQ VIHSGVGGIT
ENDLSLVASS EHAVILGFNI RPTGNVKNKA KEYNVSIKTY TVIYALIEEM RSLLLGLMSP
IIEEEHTGQA EVRETFNIPK VGTIAGCVVS DGVITRGIKV RLIRDGVVIH TGEILSLKRF
KDDAKEVSKG YECGIMLENY NEIKVGDVFE TYKEIHKKRT L
