ID G2H161_9ENTR Unreviewed; 891 AA.
AC G2H161;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000256|HAMAP-Rule:MF_00100};
GN ORFNames=Rin_00017960 {ECO:0000313|EMBL:EGY28271.1};
OS Candidatus Regiella insecticola 5.15.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; aphid secondary symbionts; Regiella.
OX NCBI_TaxID=1005043 {ECO:0000313|EMBL:EGY28271.1, ECO:0000313|Proteomes:UP000004116};
RN [1] {ECO:0000313|EMBL:EGY28271.1, ECO:0000313|Proteomes:UP000004116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R5.15 {ECO:0000313|Proteomes:UP000004116};
RX PubMed=21948522; DOI=10.1101/gr.125351.111;
RA Hansen A.K., Vorburger C., Moran N.A.;
RT "Genomic basis of endosymbiont-conferred protection against an insect
RT parasitoid.";
RL Genome Res. 22:106-114(2012).
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:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000644}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000645}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000256|ARBA:ARBA00007733, ECO:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000644}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGY28271.1}.
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DR EMBL; AGCA01000425; EGY28271.1; -; Genomic_DNA.
DR RefSeq; WP_006707442.1; NZ_AGCA01000425.1.
DR AlphaFoldDB; G2H161; -.
DR PATRIC; fig|1005043.3.peg.1655; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000004116; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00100};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00100}; Reference proteome {ECO:0000313|Proteomes:UP000004116}.
FT DOMAIN 390..559
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 128..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..541
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 128..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 399..406
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 445..449
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 499..502
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 891 AA; 97810 MW; BAAD8880F2318717 CRC64;
MTDVTIKLLA AEISTSVDRL IQQFADAGLK KSETSSVTQQ EKEILLAHLK HEPGQVPNKL
TLQRKIRSTL NVPSSGGKSK SVQIEIRRKR TYINTPNAEL ANTEKAKTEQ VEQVKQVEQI
EQIEQVEKKP AKAEEQAKSE SAKEANAKKI ADTKSKPIVE KKKLTTQQQS DKTRREAEAA
ELKRSVEREV RRKIEEDAKR VAEEARKMAA ENEGKWPEPI AEQIELTDYH VTTSQHARAA
EDENDAKVEG DRRSRSRGSK TTKQKKGNKL SESKTDREEA RAVGRKSKRK PSTLQQSFNK
PVAAVNRDVI IGETVTVAEL ANKMAVKGSQ VIKTMMKLGG MATINQVIDQ ETAQLVAEEM
GHKVILRREN ELEEALMSDR DMGVAGESVL RAPVVTIMGH VDHGKTSLLD CIRSTKVAAG
EAGGITQHIG AYHVETENGM VTFLDTPGHA AFTSMRARGA QATDIVVLVV AADDGVMPQT
IEAIQHAKAA KVPVVVAINK IDKPNADPER LRTELSQHGI LPEEWGGDSP FVHVSAKKGT
GIDDLLNAIL LQAEVLELKA VHSGMASGVV IESFLDKGRG PVATVLVQSG TLNKGDIVLC
GFEYGRIRAM RDEMRRDIES AGPSIPVEIL GLSRVPVAGD SVTVVRDEKK AREVALYRQG
KFREVKLASQ QKLKLENMFA NMAEGEVSEL NIVLKSDVQG SCEAICHSLT QLSTHEVKVK
IVGSGVGGIT ETDATLATAS KAIIIGFNVR ADASARRVIE TENLDLRYYS VIYSLIDEVK
HAMSGMLAPE YKQQIIGLAE VRDLFKSPKF GAIAGCMVTE GTIKRSSPIR VLRDNVVIYE
GELESLRRFK DDVNEVRNGM ECGIGVKNYN DVRAGDMIEV FETIQIKRTI D
//
