ID A0A0K1NBQ5_9BURK Unreviewed; 1015 AA.
AC A0A0K1NBQ5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=ADJ79_03280 {ECO:0000313|EMBL:AKU66500.1};
OS Ottowia sp. oral taxon 894.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ottowia.
OX NCBI_TaxID=1658672 {ECO:0000313|EMBL:AKU66500.1, ECO:0000313|Proteomes:UP000056623};
RN [1] {ECO:0000313|Proteomes:UP000056623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W10237 {ECO:0000313|Proteomes:UP000056623};
RA Holder M.E., Ajami N.J., Petrosino J.F.;
RL Submitted (JUL-2015) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00100}.
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DR EMBL; CP012073; AKU66500.1; -; Genomic_DNA.
DR RefSeq; WP_050714766.1; NZ_CP012073.1.
DR AlphaFoldDB; A0A0K1NBQ5; -.
DR STRING; 1658672.ADJ79_03280; -.
DR KEGG; oto:ADJ79_03280; -.
DR PATRIC; fig|1658672.3.peg.892; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000056623; 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: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 515..684
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 93..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..666
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 136..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 524..531
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 570..574
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1015 AA; 107143 MW; 433567E8826DF75C CRC64;
MSNITVAELA NELKRSVGKL LEQLQAAGVK KSSGGDVLTE ADKKKLLDHL QSSHGTVAPA
RKKITLTKKT TSEIKQADAT GKARTIQVEV RKKRTFIKRD DEPAAAPQTP SPSPAAEAAR
PAAAAAPASP VIGAAEAARR EEEARRHAEL LRRQEAEAAE KRRLREEQDA RRQAEAAQPG
PEEAKPQETP AAPQTPAPQA PAADSGLLPA PAATQTKPSK TAEPETVSES ALEAVSSAAP
ASGSAPAKET AAPAARKAAT GGAAKLASSS AASSSAASPD AAPAAVAEPA KPSPEEEAAR
RREQEERRRK AMAEAEAIRS MMNKPRKVLV AKKPESAKKA AEASKDGGKP AKTGGASSAR
QGSAPAGGSK EVKSAKLSSS WAGEPGKKKG IPTRGDASGG VGRNNWRSGP KSRRSERDSQ
QAAQAAPAEH RVLEVHVPET ISVAELAHKM AVKASEVIKT LMKMGQMVTI NQPLDQDTAM
IVVEEMGHTA VVAALDDPEA FTDEEVQAQS AEALPRAPVV TVMGHVDHGK TSLLDYIRRA
KVAASEAGGI TQHIGAYHVK TPRGIVTFLD TPGHEAFTAM RARGAQATDI VILVVAADDG
VMPQTREAIK HAKAAGVPIV VALTKADKPE ANVERVTSEL VAEEVVPESY GGDSPFIAVS
SKTGMGIDDL LENVLLQADV LELKAPVEAA AKGLVIEARL DKGRGPVASV LVQSGTLKVG
DVVLAGQTSG RVRAMLNEDG KPVKEAGPSI PVEIQGLADV PQAGDEFMVL ADERRAREIA
TYRAGKFRNT KLARQQAAKL ENVFADMSAD EVKQLPIIIK ADVQGSQEAL SASLLKLSTD
EVKVQVVYAA VGGISESDVN LAIASNAIVL GFNVRAEAGA RKLAEANDVE IRYYNIIYDA
VDDLKAAMSG MLAPEQKEEV IGSAEIRTVF VASKIGTVAG SYVTSGVVRR DAHFRLLRDH
VVIYTGELES LKRMKDDVRE VKEGFECGIK LKNYNDIREG DQLEFFEIKE IARTL
//
