ID A0A095U9P8_9BURK Unreviewed; 1016 AA.
AC A0A095U9P8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=JL37_29850 {ECO:0000313|EMBL:KGD85659.1};
OS Achromobacter sp. RTa.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=1532557 {ECO:0000313|EMBL:KGD85659.1, ECO:0000313|Proteomes:UP000035841};
RN [1] {ECO:0000313|EMBL:KGD85659.1, ECO:0000313|Proteomes:UP000035841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RTa {ECO:0000313|EMBL:KGD85659.1,
RC ECO:0000313|Proteomes:UP000035841};
RA Prabhakaran M., Cougar B., Weirick T., Fathepure B.Z.;
RT "Genome sequences of the lignin degrading proteobacteria.";
RL Submitted (AUG-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:KGD85659.1}.
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DR EMBL; JPYO01000047; KGD85659.1; -; Genomic_DNA.
DR RefSeq; WP_043549029.1; NZ_JPYO01000047.1.
DR AlphaFoldDB; A0A095U9P8; -.
DR eggNOG; COG0532; Bacteria.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000035841; 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; 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; 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}.
FT DOMAIN 517..686
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 106..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..668
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 194..208
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 526..533
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 572..576
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 626..629
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1016 AA; 107409 MW; AB57C26781A0D8F2 CRC64;
MSSNTVAQFA TELKMPANVL LDQLRSAGVD LKSVDDAVTD SDKAKLLESL RRAHGATEGK
KITLTRRQTS EIRQADATGR SRTIQVEVRK KRVFVKRDPS EIALEQAASA RAEDEASVEE
AQQVSAPAAP EAPAVAEPRE AAPAVQAEAP APAKAEEPAA VEAPAPVEAP APVESVAAEV
PAPVEAKPAE VQAQPEPEPT PAPAPAEPVA QEAKPEVKTE STEPKAEEAK PEPVVLANKS
EPTSSQAAAP AAQAEQPAAK SEPVKAAAPQ SAAQPAAKVG NRADNRRAAP PLAASASSTA
ARDEARRAAE AEAAALREML NRPRKVLRAP EPEAPAAAPI SGTLHKPAGK PGAPGAKKDA
KPAAPGNKKT IKTAEVASTW SDDASRKKPA DKAAAPASRD GWRAGGKGGK GGGRGGRNQQ
NDRRNEPAPQ EFIAREVHVP ETISVADLAH KMSVKAAEVI KQLMKLGQMV TINQVLDQET
AMIVVEELGH VAIAAKLDDP EAFLDESAAG TEAEMLPRAP VVTVMGHVDH GKTSLLDYIR
RAKVAAGEAG GITQHIGAYH VQTERGMVTF LDTPGHEAFT AMRARGAKAT DIVILVCAAD
DGVMPQTREA IHHAKAAGVP MVVAMTKIDK PTANPDRVKQ ELVAEEVVPE EYGGDVPFVS
VSAKTGEGID DLLENVLLQA EVLELKAPVD APAKGLVIEA RLDKGRGPVA TILVQSGTLH
RGDVVLAGAS FGRVRAMLDE NGKPIQEAGP SIPVEIQGLT EVPAAGDELM VLSDERKARE
IALFRQGKFR DVKLARQQAA KLESMFDNLG EGTQTLALIV KTDVQGSQEA LVQSLTKLST
DEVRVQVVHA AVGGISESDI NLAIASNAVV IGFNVRAEAS AKKLAETNGI DVRYYNIIYD
AVDEVKAAMS GMLAPEKKEE VIGLVEIREV YSISRIGNIA GCMVLDGLVR RDSQVRLLRN
NVVHWTGQLD SLRRFKDDVK EVKSGFDCGL TLRGNNDIQV GDQLEVFEIK EIARTL
//
