ID A0A1G8XGJ5_9GAMM Unreviewed; 923 AA.
AC A0A1G8XGJ5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN05216212_1091 {ECO:0000313|EMBL:SDJ89759.1};
OS Microbulbifer yueqingensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Microbulbiferaceae; Microbulbifer.
OX NCBI_TaxID=658219 {ECO:0000313|EMBL:SDJ89759.1, ECO:0000313|Proteomes:UP000199305};
RN [1] {ECO:0000313|EMBL:SDJ89759.1, ECO:0000313|Proteomes:UP000199305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10658 {ECO:0000313|EMBL:SDJ89759.1,
RC ECO:0000313|Proteomes:UP000199305};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FNFH01000002; SDJ89759.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8XGJ5; -.
DR STRING; 658219.SAMN05216212_1091; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000199305; 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 Coiled coil {ECO:0000256|SAM:Coils};
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}.
FT DOMAIN 423..592
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 97..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..574
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COILED 678..711
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 112..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 432..439
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 478..482
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 532..535
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 923 AA; 100778 MW; 595F6B66DDD21ACB CRC64;
MAEVTVSELA KSVGATEDRL LKQMKDAGLP HTSADAMVSD EEKQVLLNFL KSSHGEQEAS
APRKITLKRK TTTTLKTGSG TGRKTVNVEV RKKRTYVKRP EAEQAAESAV EAQRAELEKA
LAEQAEQERA RAEQAEAERA RAEAEAKAAA EAAAEQQAEV AAEEQPEEPA EVAAEAGEEA
PGSGEEAEQA KPAPVRSTYV DDIEAMRIAA MERRKVQTAR EEQELEEKKA RLEEERQRAE
KEKQEREEKA KAAGAVKPSL RRKLEATPVT ADKDEDEPRK RRGRKTKGGP KKSSKTALYE
QALEAFEDDE SEKRSTRSLS RPTLKIKNTH GFKKPTGKQV YEVQLGETIT VGDLAKQLNM
KAGELIKRLM KMGEMVTINQ PIDRDTATLI VEELGHKVVL RSENELEESL VAEVERAEGE
EVSRAPVVTV MGHVDHGKTS LLDYIRKTKV ASGEAGGITQ HIGAYRVQTS QGEVAFLDTP
GHAAFTAMRA RGAQATDVVI LVVAADDGVM PQTEEAIQHA KAAGVPLVVA INKCDKEGAD
PDRVKNELAA KDVIPEDWGG DTQFIEVSAH TGQGIDELLE AVSLQAEMLE LKSEVGVPAR
GVVIESRLEK GRGVVATLLV QSGELKRGDI VLAGQSYGRV RAMTNELGKS VKEAGPSTPV
ELLGLDTTPN AGDEFMVVAD ERKAREVAEQ RAEKERRERM QRQQAAKLEN MFADMEAGER
KVLPVVIKAD VRGSLEAILS ALADIGNEEV SVNVVSSGVG GIAENDVNLA LTAGAIIIGF
NTRADVTARK LAETESVEIR YYSVIYNLLD EVKQALSGML EPEVREEIVG IAEVRDVFRS
PKFGAIAGCM VTEGTVYRNK PIRVLRDNVV IYQGELESLR RFKDDVQEVR NGMECGIGVK
DYNDVKPGDQ IEVFDIVKVA REL
//
