ID A0A165NMM5_9GAMM Unreviewed; 904 AA.
AC A0A165NMM5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=A3709_11375 {ECO:0000313|EMBL:KZX50347.1};
OS Halioglobus sp. HI00S01.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Halioglobus.
OX NCBI_TaxID=1822214 {ECO:0000313|EMBL:KZX50347.1, ECO:0000313|Proteomes:UP000077184};
RN [1] {ECO:0000313|EMBL:KZX50347.1, ECO:0000313|Proteomes:UP000077184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI00S01 {ECO:0000313|EMBL:KZX50347.1,
RC ECO:0000313|Proteomes:UP000077184};
RA Sosa O.A.;
RT "Microbial cycling of marine high molecular weight dissolved organic
RT matter.";
RL Submitted (MAR-2016) 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:KZX50347.1}.
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DR EMBL; LWEE01000413; KZX50347.1; -; Genomic_DNA.
DR RefSeq; WP_066059870.1; NZ_LWEE01000413.1.
DR AlphaFoldDB; A0A165NMM5; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000077184; 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; 1.
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:UP000077184}.
FT DOMAIN 404..573
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 146..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..555
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 183..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 413..420
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 459..463
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 513..516
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 904 AA; 96632 MW; 4305003FC74031D7 CRC64;
MAQVTVQQLA EVVGASTERL LTQMKEAGLP HTDAAEAVSD EDKQTLLAFL KRSHGESTDA
PKRITLKRKT LSTLKTSGSQ GKKTVAVEVR KKRTYVKRDP AEIEAEAAAA AEAAAEEAVA
VEKAAEEAAA AEAAAAEAAE AAEKAAAEAA AAEAEAAEAE AEAAAAEAAA PAEDAEVEED
PANIDPEVLR QRAAARRKKQ EAEQAAARKA ALEAKKAEEE RKKAEAAAKA KEAASKDATK
RPKRLHDAPT TTTVDRKKKP HARPDRNAPQ GRGKQRGHNL SLSDLDRAES GMGRRRGRKK
LKAAHEEHSK HGFELPTAKK AVEVEVGEMI SVGDLAAQMS IKAGEVIKQL MGLGVMATIN
QMIDQDTATL VVEELGHSVK AVSSEALEES LEESLAQHEG TEESRAPVVT VMGHVDHGKT
SLLDYIRKSH VASGEAGGIT QHIGAYHVET DHGMISFLDT PGHAAFTAMR ARGAKSTDIV
ILVVAADDGV MPQTEEAVNH ARAAEVPLIV AVNKMDKEGA DPDRVKNELA AKDVIPEDWG
GDVQFIPVSA LTGEGISELL DAVLLQSEML ELTAARDVPA QGIVIESRLD KGRGSVASLL
VQSGTLRQGD IVLAGLQYGR VRAMLDENGQ PIKEAGPSIP VEILGLDGTP DAGDQFAAVE
NERQARELAD FRQEKSRDTK LARQQAAKLD NMFEAMGAGD RKTLNVVVKA DVRGSLEAIQ
ASLLDLGNDE VQVNIVSGGV GGITETDVTL AITSNAVMFG FNVRADASAR KVVENEGVDL
RYYNVIYDLL DDVKSALSGM LAPELREEIV GIAEVRDVFR SPKFGQIAGC MVTEGTVYRS
KPIRVLRDSV VIYEGELESL RRFKDDANEV RNGMECGIGV KNYTDVKVGD QIEVYEVKEI
ARSL
//
