IF2_SYNAS
ID IF2_SYNAS Reviewed; 919 AA.
AC Q2LWU6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SYNAS_26760;
GN ORFNames=SYN_01787;
OS Syntrophus aciditrophicus (strain SB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophales; Syntrophaceae;
OC Syntrophus.
OX NCBI_TaxID=56780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB;
RX PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA Campbell J.W., Gunsalus R.P.;
RT "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT of microbial growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
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 -!- SEQUENCE CAUTION:
CC Sequence=ABC78555.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000252; ABC78555.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041585107.1; NC_007759.1.
DR AlphaFoldDB; Q2LWU6; -.
DR SMR; Q2LWU6; -.
DR STRING; 56780.SYN_01787; -.
DR EnsemblBacteria; ABC78555; ABC78555; SYN_01787.
DR KEGG; sat:SYN_01787; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_7; -.
DR OrthoDB; 79180at2; -.
DR Proteomes; UP000001933; 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..919
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335516"
FT DOMAIN 420..589
FT /note="tr-type G"
FT REGION 93..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..436
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 454..458
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 475..478
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 529..532
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 565..567
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 158..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 429..436
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 475..479
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 529..532
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 919 AA; 101214 MW; CF314771D7330006 CRC64;
MSKKRVYELA RELGIDNKEL ISRLEKLGIA VKSHSGTLED SEVDRVTKEF HARGSREMVE
QRIKTTVIRR RAVRVPEKEA VLEKVPVEME KEMGKALPEE VPEKIAPSRE TPPAKVVKPR
PVVPEKKIPA AGEKPLAPPE KPAEPVAPPI AEILKQEKIQ PPEKFAEEPL KKPAVIEPEK
AAAAPKAVPG EAKPLPRTER VQEQGKPVPG RKEGRTPVSR RPAETRFPAK PAPQPEMARK
QVVAAAPGRA VPQEKGAPKT EAEKPRKKIK LPDETRKGEQ IPARKKTVLK KGPEKTDFRG
TLEEEIIERA VRPPRWKEEK KAAPVKMKKT EITVPKAIKR RIRVGEAITV GDLAKKMGVK
AGEVINKLMR MGLMATINQS IDFDAASLIA TEFEYQVEPA GMEYDESMFK VESSVENLKP
RAPVVTIMGH VDHGKTSLLD AIRKTRVTEG EAGGITQAIG AYRVNLKGRE IVFLDTPGHE
AFTAMRARGA QVTDIVVLVV AADDGVMDQT VEAINHSKIA GVPIIVAINK IDKPEADPGR
IKQALTEYEL VPEEWGGDTI FSEVSAKQKI GIEELLELIL LQADVLELKA DPDRPARGVV
IEARLDRGRG PVATVLIQEG TLHEGDAFVS KTEYGRVRAM NDDQGRRIKE AGPATPVEVI
GFSRVPQASA EFNAVEDEKK ARSIGDYWMR KEREKELSAT SKITLEQLYE KMKEGVKELN
VILRADVQGS LEALSDALTK LSTDDIKLKV IHGSTGAITE TDVMLASASN AIIIGFNVRP
DARVAEIAEA EGVDIKLYDI IYNVIADVRA AMEGLLEPEY REVVLGRAEV RDLFRVPKVG
TVAGSFVIDG KVTRKANVKL VRDGVVVFDG KIGSLKRFKD DVKEVLSGFE CGIGIEGFND
LRMGDMIEAY INEKVERKL
