IF2_HELPS
ID IF2_HELPS Reviewed; 948 AA.
AC B2USN4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=HPSH_02080;
OS Helicobacter pylori (strain Shi470).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=512562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shi470;
RA Kersulyte D., Kalia A., Gilman R.H., Berg D.E.;
RT "Genome sequence of Helicobacter pylori from the remote Amazon: traces of
RT Asian ancestry of the first Americans.";
RL Submitted (MAY-2008) 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; CP001072; ACD47866.1; -; Genomic_DNA.
DR RefSeq; WP_001293395.1; NC_010698.2.
DR AlphaFoldDB; B2USN4; -.
DR SMR; B2USN4; -.
DR KEGG; hps:HPSH_02080; -.
DR HOGENOM; CLU_006301_4_0_7; -.
DR OMA; VIFAMNK; -.
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..948
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093793"
FT DOMAIN 447..616
FT /note="tr-type G"
FT REGION 61..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..463
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 481..485
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 502..505
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 556..559
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 592..594
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 91..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 456..463
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 502..506
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 556..559
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 948 AA; 105862 MW; 0F841675C66341C3 CRC64;
MSEMVDLKKF LTELGKTQKE LKNVIEQAKD IGLELKTNSK MTPEQAGKLY KYIVDGIKEQ
IQANKPTKNP EQDNKDDLNI TATPKPLNKK VSKTPKKEET KSQPKPKKTK EKKKEAPALI
AKKKGGIEIV NTFEDQTLEN TPKVVSHSQI EKAKQKLQEI QKSREALSKL TQSNTNNANS
TNNANNVNNA KKEISEVKKQ EQEIKRHENI KRRTGFRVIK RNDETENETE NSVAESKKPT
QSAAAIFEDI KKEWQEKDKQ EAKKAKKPSK PKATPTAKNN KSHKIDFSDA RDFKGNDIYD
DETDEILLFD LHEQDNLNKE EEEKEIRQNI NDRVRVQRKN PWMNESGIKR QSKKKRAFRN
DNSQKVIQSA ISIPEEVRVY EFAQKANLNL ADVIKTLFNL GLMVTKNDFL DKDSIEILAE
EFHLEISVQN TLEEFEVEEV LEGVKKERPP VVTIMGHVDH GKTSLLDKIR DKRVAHTEAG
GITQHIGAYM VEKNDKWVSF IDTPGHEAFS QMRNRGAQVT DIAVIVIAAD DGVKQQTIEA
LEHAKAANVP VIFAMNKMDK PNVNPDKLKA ECAELGYNPV DWGGEYEFIP VSAKTGDGID
NLLETILIQA DIMELKAIEE GSARAVVLEG SVEKGRGAVA TVIVQSGTLS VGDSFFAETA
FGKVRTMTDD QGKSIQSLKP SMVALITGLS EVPPAGSVLI GVENDSIARL QAQKRATYLR
QKALSKSTKV SFDELSEMVA NKELKNIPVV IKADTQGSLE AIKNSLLELN NEEVAIQVIH
SGVGGITEND LSLVSSSEHA VILGFNIRPT GNVKNKAKEY NVSIKTYTVI YALIEEMRSL
LLGLMSPIIE EEHTGQAEVR ETFNIPKVGT IAGCVVSDGV IARGIKARLI RDGVVIHTGE
ILSLKRFKDD VKEVSKGYEC GIMLDNYNEI KVGDVFETYK EIHKKRTL
