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IF2_HAHCH
ID   IF2_HAHCH               Reviewed;         861 AA.
AC   Q2SML3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=HCH_01239;
OS   Hahella chejuensis (strain KCTC 2396).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Hahella.
OX   NCBI_TaxID=349521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 2396;
RX   PubMed=16352867; DOI=10.1093/nar/gki1016;
RA   Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA   Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA   Oh T.K., Kim J.F.;
RT   "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT   algicidal agent.";
RL   Nucleic Acids Res. 33:7066-7073(2005).
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; CP000155; ABC28111.1; -; Genomic_DNA.
DR   RefSeq; WP_011395184.1; NC_007645.1.
DR   AlphaFoldDB; Q2SML3; -.
DR   SMR; Q2SML3; -.
DR   STRING; 349521.HCH_01239; -.
DR   PRIDE; Q2SML3; -.
DR   EnsemblBacteria; ABC28111; ABC28111; HCH_01239.
DR   KEGG; hch:HCH_01239; -.
DR   eggNOG; COG0532; Bacteria.
DR   eggNOG; COG3064; Bacteria.
DR   HOGENOM; CLU_006301_6_1_6; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000000238; 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; 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; PF11987; IF-2; 1.
DR   Pfam; PF08364; IF2_assoc; 1.
DR   Pfam; PF04760; IF2_N; 1.
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..861
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000335478"
FT   DOMAIN          362..531
FT                   /note="tr-type G"
FT   REGION          107..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          371..378
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          396..400
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          417..420
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          471..474
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          507..509
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        107..131
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..232
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..261
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         371..378
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         417..421
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         471..474
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   861 AA;  93752 MW;  681BBB6A88F27012 CRC64;
     MAEVTIKQLA EDVGAPVERL LKQMVDAGLE KRGEGDIVTD SEKQKLLAFL KQSHGESFSE
     PKKITLKRKT TTTLKASGTG ANRSINVEVR KKRTYIKRSE AVNDIDAQKQ QDIQRAAEEA
     AAKERETEVE VALQNEPGME ATAEVVESVQ QEAANMDTQE AEAAPQASVD ESVSATTAGG
     SQEKAGVAAD QEAEDAQKSE ARKTSKHRRN KEDSEVRREP ADAEDLKRRE KHKPKPAPQL
     KSSKVIAIEE DDSSEEAPRR ARQRKKKSKV VQDRSVQPIV REVVISDTIT VAELAQKMSV
     KGVEVIKRLM GMGIMATLNQ SIDQDVAQLV AEEMGHKVKL LQEDAVETEV LESISFEGES
     KSRAPVVSVM GHVDHGKTSL LDYIRRAKVA AQESGGITQH IGAYHVETPR GMISFLDTPG
     HAAFTAMRAR GAQCTDIVIL VVAADDGVMP QTQEAVQHAK AAGVPLVVAV NKMDKEQADP
     DRVKNELSAL DVIPEEWGGD VQFVPVSAHT GDGIDDLLEA VLLQSEMLEL TAVPDAPGKG
     VVIESSLDRG RGSVATVLVQ NGTLRHGDIV LAGEYYGRVR AMVNENGQNV QEAGPSIPVE
     ILGLNGTPDA GDEFIVVPDE KKAREVAEFR QNKERQTRLQ RQQAASLENL FENMGKGGVK
     ELNIVLKTDV RGSLEALIGA LAEIGNEEVQ VKIIASGVGG ITETDANLAL STQAIIVGFN
     VRADASARKI VEKEGIELRY YSVIYNIIDD VKKALTGMLA PEFREDIVGT AEVRDTFKSP
     KFGQVAGCMV LEGAVYRNKP IRVLRDNVVI FEGELESLRR FKDDVAEVRA GTECGIGVRN
     YEVKVGDIIE VFDKIRVERS L
 
 
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