ID A0A411HLG1_9GAMM Unreviewed; 885 AA.
AC A0A411HLG1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=ELE36_13730 {ECO:0000313|EMBL:QBB71328.1};
OS Pseudolysobacter antarcticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudolysobacter.
OX NCBI_TaxID=2511995 {ECO:0000313|EMBL:QBB71328.1, ECO:0000313|Proteomes:UP000291562};
RN [1] {ECO:0000313|EMBL:QBB71328.1, ECO:0000313|Proteomes:UP000291562}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AQ6-296 {ECO:0000313|EMBL:QBB71328.1,
RC ECO:0000313|Proteomes:UP000291562};
RA Wei Z., Peng F.;
RT "Pseudolysobacter antarctica gen. nov., sp. nov., isolated from Fildes
RT Peninsula, Antarctica.";
RL Submitted (JAN-2019) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP035704; QBB71328.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411HLG1; -.
DR KEGG; xbc:ELE36_13730; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000291562; 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; 1.
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:UP000291562}.
FT DOMAIN 384..553
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 105..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..535
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 165..195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 393..400
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 439..443
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 493..496
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 885 AA; 95446 MW; 5A8D8943D37F4238 CRC64;
MSDVTVKQLA KVLGMTDDKL LAQLAEAGMT FNSVDQPVSS TEKVKLLGFL RRTHGKGEAA
AAETTAPRQI TLKRKTVSEI TVAGVGPRGP SKTVNVEVRQ KRTYVKRSSM TDEPEVDSER
EDALRKLQES QTKREAEDLL IQEKDKRRHD EEARLRAIED AKRQAEEGRL RAETEARAAA
EEAAKPRKEE PARVDAAPKV AATPAPAAAA APQPPRKDHR VRDAVDEPAR HKGPRAPRGR
EEGGSDEPAG KTYFGAELHL SKAGSERRGA AKKKPRPRPG EMQKQQPGGP AHGFSRPTAP
VVREVAIGES IIVADLAQKM AVKGAEVVKK LFKMGVMATI NQAIDHDTAV LVVEEMGHTA
VAEIGTDAES VLVAKTDNAG DKETRPPVVT IMGHVDHGKT SLLDYIRRTK VASGEAGGIT
QHIGAYHVET GKGVVSFLDT PGHAAFTSMR SRGAKLTDIV VLVVAADDGV MPQTIEAVQH
ARAAGVPLIV AVNKMDKPDA EADKVKQGLV QHEVVPEEWG GDTIFVPVSA KTGDGVDALL
DAILVQAEVM ELKAVKDGLA SGVVIESSLD KGRGPVATVL VQQGTLKKGD FLVCGVEYGR
VRALFDETGK QVESAGPSIP VQVLGMSGVP EAGDDFVAVA DERLAKDVAQ QRQQKRRESR
LFKKSTKLED VMSQMGNQGE TQRVLNLVVK ADVQGSVEAL RDSLTSLTND IVRVNVIASG
VGGITESDAT LAAASKAIVI GFNVRADASA RKVINESDLD IRYFSIIYDV IDQVKQAVTG
LLGTEIREDI IGTAQVRDVF RSSKFGAIAG CMIIEGTVKR NKPIRVLREN TVIYQGELES
LRRFKENVDE VRNGMECGIG VKQYNDVKPG DQIECYERVE IQRTL
//
