IF2_ACTSZ
ID IF2_ACTSZ Reviewed; 837 AA.
AC A6VNE0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Asuc_1121;
OS Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS 130Z).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=339671;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z;
RX PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA Burkhart K.B., Harkins V., Vieille C.;
RT "A genomic perspective on the potential of Actinobacillus succinogenes for
RT industrial succinate production.";
RL BMC Genomics 11:680-680(2010).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000746; ABR74487.1; -; Genomic_DNA.
DR RefSeq; WP_012072864.1; NC_009655.1.
DR AlphaFoldDB; A6VNE0; -.
DR SMR; A6VNE0; -.
DR STRING; 339671.Asuc_1121; -.
DR PRIDE; A6VNE0; -.
DR EnsemblBacteria; ABR74487; ABR74487; Asuc_1121.
DR KEGG; asu:Asuc_1121; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001114; 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; 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; 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..837
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000071285"
FT DOMAIN 337..506
FT /note="tr-type G"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..353
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 371..375
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 392..395
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 446..449
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 482..484
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 346..353
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 392..396
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 446..449
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 837 AA; 91540 MW; 56FFB4B6A310EE3C CRC64;
MTEKEQNAEN APKKLSLKRR EKTTVSATTA GGKAKAVQVE VRKSRKIDTE AAIKAAEAAK
LKAQEEAEAK AKAEAEKAEQ EKATAAKVRE KAAKPTKAEA KPENSTVAKA ADPEKEKRKA
EEAELRRKAD ELARQKAEEQ ARKAAEDAKR YAEAAKDTVE HHNDSDDFSD YHLTSSYARE
AEDEDNRRRE NHIRTGKNKV TKAKKGGRDD NGSKDERSAD RRNQKDMRGK GKQSKQGKRG
STLQQAFTKP AQVTKSDVVI GETITVAELA NKMAIKATEI IKTMMKMGEM VTINQVLDQE
TAQLVAEELG HKVILRKENE LEESVLEDRD VNAEKVQRAP VVTIMGHVDH GKTSLLDYIR
KAKVAAGEAG GITQHIGAYH VETKGKIITF LDTPGHAAFT SMRARGAKAT DIVVLVVAAD
DGVMPQTIEA IQHARAAGVP IVVAVNKIDK PEANPERVEQ ELLQYDVVAE KFGGDVQFVY
VSAKKGSGVD DLLDAILLQS EVLELTAVKD GMASGVVIES YLDKGRGPVA TILVQSGTLK
RGDIVLCGFE FGRVRAMRDE DGKDINEAGP SIPVEVLGLS GVPAAGDEAT VVRDEKKARE
VALYRQGKFR EVKLARQQKA KLENMFSNMS EGDVAELNVI VKADVQGSVE AIVQSLQELS
TEEVKVKVVG SGVGGITETD ATLAAASNAI MVGFNVRADA SARRVIENEN IDLRYYSIIY
ELLNEIKAAM SGMLQPEFKQ EIIGLAEVRD IFRHPKFGAI AGCMVTEGIV KRNNPIRVLR
DNVVIFEGEL ESLRRFKDDV NEVRNGMECG IGVKNYNDVK VGDQIEVFEV VEVKRSI
