ID A0A286EBP6_9NEIS Unreviewed; 946 AA.
AC A0A286EBP6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=SAMN02746062_01194 {ECO:0000313|EMBL:SOD68300.1};
OS Alysiella filiformis DSM 16848.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Alysiella.
OX NCBI_TaxID=1120981 {ECO:0000313|EMBL:SOD68300.1, ECO:0000313|Proteomes:UP000219669};
RN [1] {ECO:0000313|EMBL:SOD68300.1, ECO:0000313|Proteomes:UP000219669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16848 {ECO:0000313|EMBL:SOD68300.1,
RC ECO:0000313|Proteomes:UP000219669};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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}.
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DR EMBL; OCNF01000008; SOD68300.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A286EBP6; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000219669; 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; 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; 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; PF04760; IF2_N; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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|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:UP000219669}.
FT DOMAIN 446..615
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..597
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 7..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 455..462
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 501..505
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 555..558
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 946 AA; 101517 MW; 61BF1BE021E682AC CRC64;
MSNNRNNKPE VEHKGGKKVK MSREEMLAQL KAEQSAQTAK TETPATPAPA NTAPQPENAS
APLSAEDAER AAKKAAAEAE AAKLKAAKAA KSAKSETAKT VKETVADSPE TPSVSTENSS
EKQPEKAPAA PSDNAPAGEN GETKEKRKRS RGGRNRNKNK DKDGAPEAVP TLVEVVNAEE
AARREAEAEQ ERKRREAQEA LLREKQERAE RQARREAAKA QAAEEARLAA AAKKEGKDGK
GVRTAKPSEE KLAQKAAETK SPKPIAKTND KASKPAEKVA KPVSGSLNDE NPSSGSRKKD
DRRHSRDDDA PKGKGGKNVK GGRNDSRNAG GDDERVRGGN KKAKKLKLAP NQHAFQAPTE
PVVHEVLVPE TITVADLAHK MAVKGVEVVK TLMKMGMMVT INQSLDQDTA LLVVEEMGHI
GKPAAIDDPD AFLNDDSTHV DAEMLPRPPV VTVMGHVDHG KTSLLDHIRK TRVVSGEAGG
ITQHIGAYHV ETPRGVVTFL DTPGHEAFTA MRARGAKATD IVILVVAADD GVMPQTVEAI
AHAKAAGVPI VVAVNKIDKD SANPERIRQE LTQHEVVCDE WGGDVQFVDV SAKHGINIDK
LLEAVLLEAE VLELKAPVAA PAKGLIVEAK LDKGRGAVAT LLVQSGTLRK GDMLLAGTTF
GKIRAMLDEN GKPIDEAGPS IPVEILGLSD VPNAGEDALV LADEKKAREV ALFRQGKFRD
VRLAKQQAAK LENMFNNMGE NQAQNLSIII KADVQGSYEA LAGSLQKLST DEVRVQVLHS
GVGGISESDV NLAIASGALI IAFNVRADNA ARKLAETEDV EIRYYNIIYD AIDDVKAAMS
GMLSPEEKEQ ITGTVEIRQV ITVSKVGNIA GCMVTDGLVK RDSKVRLIRN NVVIHTGELS
SLKRFKDDVK EVKMGFECGL MIKNFNEIME GDQLECFDVV EVARTL
//