ID A0A0A0EHX3_9RHOB Unreviewed; 830 AA.
AC A0A0A0EHX3;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=ATO9_07780 {ECO:0000313|EMBL:KGM49895.1};
OS Pseudooceanicola atlanticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooceanicola.
OX NCBI_TaxID=1461694 {ECO:0000313|EMBL:KGM49895.1, ECO:0000313|Proteomes:UP000030004};
RN [1] {ECO:0000313|EMBL:KGM49895.1, ECO:0000313|Proteomes:UP000030004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II-s11g {ECO:0000313|EMBL:KGM49895.1,
RC ECO:0000313|Proteomes:UP000030004};
RX PubMed=25663028; DOI=10.1007/s10482-015-0398-2;
RA Lai Q., Li G., Liu X., Du Y., Sun F., Shao Z.;
RT "Pseudooceanicola atlanticus gen. nov. sp. nov., isolated from surface
RT seawater of the Atlantic Ocean and reclassification of Oceanicola
RT batsensis, Oceanicola marinus, Oceanicola nitratireducens, Oceanicola
RT nanhaiensis, Oceanicola antarcticus and Oceanicola flagellatus, as
RT Pseudooceanicola batsensis comb. nov., Pseudooceanicola marinus comb. nov.,
RT Pseudooceanicola nitratireducens comb. nov., Pseudooceanicola nanhaiensis
RT comb. nov., Pseudooceanicola antarcticus comb. nov., and Pseudooceanicola
RT flagellatus comb. nov.";
RL Antonie Van Leeuwenhoek 107:1065-1074(2015).
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 -!- 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00100}.
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:KGM49895.1}.
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DR EMBL; AQQX01000002; KGM49895.1; -; Genomic_DNA.
DR RefSeq; WP_043747433.1; NZ_CP051248.1.
DR AlphaFoldDB; A0A0A0EHX3; -.
DR STRING; 1461694.ATO9_07780; -.
DR eggNOG; COG0532; Bacteria.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000030004; 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: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; 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; 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; TRANSLATION INITIATION FACTOR IF-2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 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; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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|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:UP000030004}.
FT DOMAIN 328..498
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 337..344
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 384..388
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 438..441
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 830 AA; 89294 MW; 1B6722796CF5F765 CRC64;
MSDNDGKKTL GVRGGGSRPG NVKQSFSHGR TKNVVVETKR KRVVVPKSGA GKSGGGAGSV
GDPSKRPAGI TDAEMDRRLK AVQAAKAREA EEAAQREAEE KAREEERQRR REEAEAKERE
EREREAALKA KQEEEERAKR DAEEAAKRAA AAAAQPAPPE DGAPARKTAP ANRGAERPAR
ANDREDRGGR GKGDKSDGRR SGKLTLNQAL SGGEGGRQKS MAAMKRKQER ARQKAMGQNT
VREKVVRDVQ VPEAIMVGEL ANRMAERVAD VVKALMQNGM MVTQNQTIDA DTAELIIEEF
GHNIVRVSDA DVEDVIKEIE DKEEDLKPRA PVITIMGHVD HGKTSLLDAI RDAKVVAGEA
GGITQHIGAY QVTTDGGQVL TFLDTPGHAA FTSMRARGAQ VTDIVVLVVA ADDAVMPQTI
EAINHAKAAE VPMIVAINKC DKPEANPTKV RTDLLQHEVI VEEMSGEVQD VEVSAHTGQG
LDELLEAIAL QAELLELKAN PDRAAQGAVI EAQLDVGRGP VATVLVQSGT LRQGDVFVVG
EQWGKVRALV NDRGERVKEA GPSVPVEVLG LNGTPEAGDV LNVTSTEAQA REIAEYRENA
AKEKRAAAGA ATTLEQLMQK AKEDENVTEM PILVKADVQG SAEAIVQAME KIGNDEVRVR
VLHAGVGAIT ESDVGLAEAS GAPVFGFNVR ANAPARNAAN QKGVEIRYYS VIYDLVDDVK
AAASGLLSAE IREKFIGYAQ IKEVFKVTGV GRVAGCLVTE GVARRSAGVR LLRDDVVIHE
GTLKTLKRFK DEVSEVISGQ ECGMAFENYE DIRPDDVIEI FEREEIERTL
//