IF2_HELHP
ID IF2_HELHP Reviewed; 882 AA.
AC Q7VHF6;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=HH_1011;
OS Helicobacter hepaticus (strain ATCC 51449 / 3B1).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=235279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51449 / 3B1;
RX PubMed=12810954; DOI=10.1073/pnas.1332093100;
RA Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M.,
RA Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R.,
RA Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B.,
RA Shen Z., Weber J., Frosch M., Fox J.G.;
RT "The complete genome sequence of the carcinogenic bacterium Helicobacter
RT hepaticus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(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; AE017125; AAP77608.1; -; Genomic_DNA.
DR RefSeq; WP_011115851.1; NC_004917.1.
DR AlphaFoldDB; Q7VHF6; -.
DR SMR; Q7VHF6; -.
DR STRING; 235279.HH_1011; -.
DR PRIDE; Q7VHF6; -.
DR EnsemblBacteria; AAP77608; AAP77608; HH_1011.
DR KEGG; hhe:HH_1011; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_4_1_7; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002495; 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..882
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137208"
FT DOMAIN 381..550
FT /note="tr-type G"
FT REGION 57..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..397
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 415..419
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 436..439
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 490..493
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 526..528
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 61..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 390..397
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 436..440
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 490..493
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 882 AA; 97443 MW; 7EDC23A7A899A220 CRC64;
MEKIRLSDFA KEFGKEAKFA YEKAKEMGLS VKTPSSSLTQ EEAAALFEYI NTGVNSYIPA
NKTKDKKETK KPKKATTKTS QSAAKEKEIK KTTTTKAPKT AKKTTSEKQK DKGEQNEIEQ
DDAQFPAQAP QSKRASKKVE SNDMTAPLET KAKVGLRIVR KNDTPQEQPS MVSKKDESKK
HAPSYKELLA DTADEEYKRH KKDKSKPKVA TKHTDQKIHI LDDRDISFHS DYDDEQDEIM
LFDLNEREVR DEEEENQIRQ AITERVHIHR KNPWMNEGSI KRGGKRRKPI KTTKNVDKIK
GPISIPEEIR VYEFAELIKA ELKDVIKVLF NLGVMATKND FLDRDAIEIL SDEFELEISI
QDAPEQNIIE STPDIDSPLL ERPPVVTIMG HVDHGKTSLL DYIRNSRIAS GEAGGITQHI
GAYMVEKNGK KISFIDTPGH EAFTQMRSRG AQVTDIAIIV IAADDGVKQQ TIEALNHAKA
ANVQIIIAMN KMDKENANPD KLKAECAEIG FTPNEWGGEY EFIPISAKNG DGVENLLETI
LIQAEVLELK ASHQGRAKAI VLEASLEKGR GPVATIIMQQ GILNVGDSVV ADTAFGRVRA
LLDDRGQNIS QLSPSGVAVV TGLSEVPSAG AIFQSVENDT IAREHAQKRA LYLRQKELSK
STKVTFDELG EMVAQGNLKT LPLIIKADTQ GSLEAIKASL EKLSNDEVRI NIIGFGVGGI
SESDITLCAT STNSLILGFN VRPTGSVKAK AKELGVEIKT YSIIYALLDD IKALLSGLMS
PIVEEENTGQ AEVRETFNIP KVGTIAGCMV VDGSIQRGIK VRLIRDGVVV HTGAISSLKR
FKDDAKEVSK GYECGIMLEN HNDIKVGDVF ETYKEITKTK IL
