ID IF2_THISH Reviewed; 853 AA.
AC B8GP02;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, 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=Tgr7_1003;
OS Thioalkalivibrio sulfidiphilus (strain HL-EbGR7).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=396588;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-EbGR7;
RX PubMed=21475584; DOI=10.4056/sigs.1483693;
RA Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N.,
RA Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7.";
RL Stand. Genomic Sci. 4:23-35(2011).
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; CP001339; ACL72091.1; -; Genomic_DNA.
DR RefSeq; WP_012637575.1; NC_011901.1.
DR AlphaFoldDB; B8GP02; -.
DR SMR; B8GP02; -.
DR STRING; 396588.Tgr7_1003; -.
DR KEGG; tgr:Tgr7_1003; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000002383; 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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.56.50; Putative DNA-binding domain, N-terminal subdomain of bacterial translation initiation factor IF2; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR004161; EFTu-like_2.
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 NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 2.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46955; Putative DNA-binding domain; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
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..853
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000190641"
FT DOMAIN 353..522
FT /note="tr-type G"
FT REGION 51..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..369
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 387..391
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 408..411
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 462..465
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 498..500
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 51..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 362..369
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 408..412
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 462..465
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 853 AA; 91668 MW; E361225595A15598 CRC64;
MTDVTVKQLS EVVGTPVERL IEQLGEAGVS VSDADQTVTE EQKLKLLEHL RKSHGKSSAA
GEGKKITLRR KSTTELRVTG SQGRAKTVSV EVRKRRTYVK RDEAEVAAPV EEAAPAPVLE
SKAAQIAKQV EEERKAAMDA SRRADEERKA AEAARKAEQE RKAAEEAARL EAEEAARREA
EEAARAAEPE TVAEAVEAAV APPPSDAARP ARRRRGPKER EDEKGGRREE LHVASDKRGR
RKGKGKGATR VAAAAVASKH GFERPTAPVV REVALPETLT VGELAQKLAI KAPELIKSLM
GMGVMATINQ AIDRDTATLV VEELGHVAVP MQVEDLDEEL AVATAEPVGE LKPRPPVVTI
MGHVDHGKTS LLDYIRSSRV ASGEAGGITQ HIGAYHVQTN RGGITFLDTP GHAAFTAMRA
RGAKVTDIVI LVVSADDGVM PQTIEAVQHA KAAGVPMVVA VNKIDKPEAD PDRVKNELSV
HQVIPEEWGG DTQFIHVSAL KGTGVEDLLE AVNLQAEVME LKAPVEGPAA GVVIESRLDK
GRGPVATVLV QRGTLNKGDV ILTGQEFGRV RAMFDENGKP VKSAGPSMPV EVLGLSGTPN
AGDDVLVLED ERKAREVALF RQGKFRESKL ATQQAAKLEN LFSQMQEGQV GTVNILLKAD
VQGSAEAIRD ALEKLSTDEV KVKIIAAGVG GITESDINLA KASEAIVIGF NVRADAGARK
AVAEQEVDLR YYSVIYEAID DVRQALTGLL SPEMREEIIG LAQVKDVFKS SQFGAVAGCL
VVEGTIKRGN PIRVLRNNVV IYEGELESLR RFKDDVNEVR AGTDCGIAVK NYNDVKPGDQ
IEVYQRVEVA RTL
//
