ID H5WNB7_9BURK Unreviewed; 955 AA.
AC H5WNB7;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
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=BurJ1DRAFT_2675 {ECO:0000313|EMBL:EHR71503.1};
OS Burkholderiales bacterium JOSHI_001.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX NCBI_TaxID=864051 {ECO:0000313|EMBL:EHR71503.1, ECO:0000313|Proteomes:UP000004674};
RN [1] {ECO:0000313|EMBL:EHR71503.1, ECO:0000313|Proteomes:UP000004674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JOSHI_001 {ECO:0000313|EMBL:EHR71503.1,
RC ECO:0000313|Proteomes:UP000004674};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Zeytun A., Lu M., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Smith J., Lewis G.,
RA Woyke T.;
RT "Noncontiguous Finished sequence of Burkholderiales bacterium JOSHI_001.";
RL Submitted (NOV-2011) 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; CM001438; EHR71503.1; -; Genomic_DNA.
DR AlphaFoldDB; H5WNB7; -.
DR STRING; 864051.BurJ1DRAFT_2675; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_4; -.
DR OrthoDB; 9811804at2; -.
DR BioCyc; BBAC864051:G1H30-2670-MONOMER; -.
DR Proteomes; UP000004674; 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 {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:UP000004674}.
FT DOMAIN 455..624
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 103..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..606
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 112..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 464..471
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 510..514
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 564..567
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 955 AA; 102251 MW; C0AD58FAF5F7D0CD CRC64;
MAVTTVAQFA AELNRPAGTL LEQLQSAGVA KKSLDDALTD ADKERLLEYL RNAHGTSADR
KKITLTRKST SEIKQADASG KARTIQVEVR KKRVFVKRDD APGAVEEPVA PAVDEEDLRR
REEEAMQQAE ALRREAEELA QRQREEQERR EREAAEAAAR AEAEAAAARE AAEAAAAKAA
ADAATRAQQA KPTDKSAPAA AKPAEVAAPV APPKPVEPPK PALRVVKAVD IDAAEKQRIV
DLDKRRKAAE AEAAAIRAMM NAPKKVMVAA KKPEEAKPVA ADLKGTIHKP KGAPGATATP
GSTVAKPGDK KSVKSEKLSS SWADDAAKKR ALKTRGDTGG GNRPGWRSPR GSRKGDRNDD
APAFNAPAEP QIQEVHIPET ISVADLAHKM SVKASEVIKQ MMKLGQMVTI NQQLDQETAM
IVVEEMGHKA LAAKLDDPEA FSEEEAAAQT GELISRAPVV TVMGHVDHGK TSLLDYIRRA
RVAAGEAGGI TQHIGAYHVE TPRGMITFLD TPGHAAFTAM RARGAKATDI VILVVAADDG
VMPQTKEAIH HAKAAGVPIV VAMNKIDKPE ANVERLKSEL VAEQVVPEDF GGESPFVAVS
AKTGQGVDDL LEQVLLQAEV LELKAPTEAA ARGLVVEAQL DKGRGPVATV LIQSGTLRRG
DVVLAGASYG RVRAMLDEDG KAIQEAGPSI PVEIQGLTEV PQAGDEFMVL TDERRAREIA
TFRQGKYRDV KLAKQQAAKL ENMFETMGAG SAQTLSLIIK ADVQGSQEAL ASSLLKLSTD
EVKVQIVHAA VGGISESDVN LGIASKAVII GFNTRADAGA RKLAEHTGVD IRYYNIIYDA
VDEVKAAMTG MLAPEQKEEV IGMAEIRTVF VASKIGTVAG CMVTNGKVTR NARFRLLRDN
VVIYTGELES LKRMKDDVRE VAEGFECGIK LKNFNDIKEG DQLEVFEVKE VARTL
//
