ID A0A069PSW7_9BURK Unreviewed; 985 AA.
AC A0A069PSW7;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 53.
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=BG61_29235 {ECO:0000313|EMBL:KDR43858.1};
OS Caballeronia glathei.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=60547 {ECO:0000313|EMBL:KDR43858.1, ECO:0000313|Proteomes:UP000027466};
RN [1] {ECO:0000313|EMBL:KDR43858.1, ECO:0000313|Proteomes:UP000027466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 50014 {ECO:0000313|EMBL:KDR43858.1,
RC ECO:0000313|Proteomes:UP000027466};
RA Liu X.Y., Li C.X., Xu J.H.;
RT "Draft Genome Sequences of Four Burkholderia Strains.";
RL Submitted (MAR-2014) 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 -!- 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:KDR43858.1}.
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DR EMBL; JFHC01000005; KDR43858.1; -; Genomic_DNA.
DR RefSeq; WP_035934006.1; NZ_JFHC01000005.1.
DR AlphaFoldDB; A0A069PSW7; -.
DR STRING; 60547.GCA_000751215_03627; -.
DR Proteomes; UP000027466; 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; 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; 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; 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:UP000027466}.
FT DOMAIN 485..654
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 104..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..636
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 104..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 494..501
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 540..544
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 594..597
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 985 AA; 106136 MW; 09CF3D8CC4197ED4 CRC64;
MASNNVAQFA AELKMPAGVL LEQLQAAGVQ KASADDDLSE MDKARLLDHL RKSHGSADAD
KRKITLTRRH TSEIKQSDAT GKARTIQVEV RKKRVFVKRD EHGAEQVVEA GNHAEDEVDE
AELQRREEEA RHAAELLEKE AQELKERQER LEREEAERRA REEAAEAERR RAEEEAAKRA
AAQAEAAEVS RAAAAVRQEP RADVRAEKKA EEPAPADNAA RQNEEKAAAE RAAQREAAKK
AEDAARAATE KARAEQEQIA KRRAAAEAEA RAIREMMNTP RRAQQAKPAE PPPAAKPAEA
AKPAEAKGTL HKPAKPEGAV SARPAAAKKP AAGAPAPAAP SAADKKKPGK GGWQDDAAKR
RGIKTRGDTS GGVDRGWRGG PKGRGKHQEQ TTFQAPTEPI VREVHVPETI SVADLAHKMS
VKASEVIKVM MKLGQMVTIN QVLDQETAMI VVEELGHRAV AAKLDDPEAL LTEGETTEEA
GERLPRPPVV TVMGHVDHGK TSLLDYIRRA KVAAGEAGGI TQHIGAYHVD TPRGVITFLD
TPGHEAFTAM RARGAKATDI VILVVAADDG VMPQTKEAIA HAKAGGVPIV VAINKIDKPD
AHSERVKQEL VAEGVVPEEY GGDSPFVEVS AKTGQGIDDL LENVSLQAEV LELTAPVEAP
AKGLVIEAKL DKGKGPVATI LVQSGTLNRG DVVLAGSAYG RVRAMLDETG KPTKTAGPSI
PVEIQGLSEV PGAGEEVIVL PDERKAREIA LFRQGKFRDV KLAKQQAAKL ENMLEQMGEG
EVQNLPLIVK ADVQGSQEAL VQSLQKLSTN EVRVQIVHSA VGAISESDVN LATASKAVII
GFNTRADAQA RKLAESNGID IRYYNIIYDA VDEVKAAMSG MLSPEKREVV TGMVEVRQVI
RVPKVGLIAG CMVTDGFVKR SSSVRVIRNN VVIHTGELDS LKRFKDDVKE VRQGFECGMS
IKNFNDIVEG DQFEIFEVTE VARTL
//