ID A0A0Q3S008_9BACI Unreviewed; 792 AA.
AC A0A0Q3S008;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=AN959_06520 {ECO:0000313|EMBL:KQL35552.1};
OS Psychrobacillus sp. FJAT-21963.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Psychrobacillus.
OX NCBI_TaxID=1712028 {ECO:0000313|EMBL:KQL35552.1, ECO:0000313|Proteomes:UP000051878};
RN [1] {ECO:0000313|EMBL:KQL35552.1, ECO:0000313|Proteomes:UP000051878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-21963 {ECO:0000313|EMBL:KQL35552.1,
RC ECO:0000313|Proteomes:UP000051878};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (SEP-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|ARBA:ARBA00025162, ECO:0000256|HAMAP-
CC Rule:MF_00100, 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:KQL35552.1}.
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DR EMBL; LJIY01000002; KQL35552.1; -; Genomic_DNA.
DR RefSeq; WP_056829315.1; NZ_LJIY01000002.1.
DR AlphaFoldDB; A0A0Q3S008; -.
DR PATRIC; fig|1712028.3.peg.2568; -.
DR Proteomes; UP000051878; 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; 1.10.10.2480; -; 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; 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; 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; 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:UP000051878}.
FT DOMAIN 294..463
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 52..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..445
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 53..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 303..310
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 349..353
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 403..406
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 792 AA; 86378 MW; 9B8A83284644830B CRC64;
MTKIRVHEYA KQIEKSSKEV IEQLGKLNIQ VANHMSMLEG DAVKKLDSVY KKSTETTKNT
AQSTPQTSTK SQQVGQSNRP SNQGQSRPSN QGQSKPTGQG QSKPSNQGSR PSNQGQSRPS
NQGQSRPSNQ GQARPSNQGQ SSQGNTSQGN TSQGSNNYSK DKKPFNNNRP GGQNRPGGQN
RPGQKFQKRR KGPTTPVQPP VPRKERELPE KITFTESLTV TELAKKLGRE PSEIIKKLFL
LGVMATINQE LDKDAIELIC ADYGVEVEEE IKIDITDLEV HFESTEDDEA NLKERPPVVT
IMGHVDHGKT TLLDSIRHTK VTAGEAGGIT QHIGAYQIVD NGKKITFLDT PGHAAFTTMR
ARGAKVTDIT ILVVAADDGV MPQTVEAINH AKAAEVPIIV AVNKMDKPSA NPDRVMQELT
EHGLVPEAWG GETIFVPISA LKGEGIDNLL EMVLLVSEVA ELKANPKRLA LGTVIEAQLD
KGRGSVATLL VQDGTLRIGD PIVVGHAYGR VRAMVNDLGR RVKEAGPSTP VEITGLNEVP
QAGDRFVVFE DEKTARQVGE TRASQAQVNQ RSEKTRVTLD NLFDQMKQGE MKELNIIVKA
DVQGTVEAMA ASLMKIEVAG VNVRIIHTGA GAITESDVTL AAASNAIVIG FNVRPDVNAK
RAADQEGVDI RLHRVIYKVI EEIESAMKGL LDPEFQEKII GQAEVRETFK VSKVGTIAGS
YVTEGKISRD SGVRIIRDSI VIFEGELDTL KRFKDDAKEV AKGYECGITI KNFNDIKEND
IIEAFIMEEI KR
//
