ID A0A0F3RRF7_9LACO Unreviewed; 794 AA.
AC A0A0F3RRF7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=VC81_09845 {ECO:0000313|EMBL:KJW12189.1};
OS Levilactobacillus spicheri.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=216463 {ECO:0000313|EMBL:KJW12189.1, ECO:0000313|Proteomes:UP000033491};
RN [1] {ECO:0000313|EMBL:KJW12189.1, ECO:0000313|Proteomes:UP000033491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LP38 {ECO:0000313|EMBL:KJW12189.1,
RC ECO:0000313|Proteomes:UP000033491};
RA Zheng J., Ganezle M.;
RL Submitted (MAR-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:KJW12189.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JZCR01000021; KJW12189.1; -; Genomic_DNA.
DR RefSeq; WP_045807910.1; NZ_JZCR01000021.1.
DR AlphaFoldDB; A0A0F3RRF7; -.
DR STRING; 216463.VC81_09845; -.
DR PATRIC; fig|216463.3.peg.1226; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000033491; 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.
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}.
FT DOMAIN 295..464
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 26..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..446
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 55..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..186
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 304..311
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 350..354
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 404..407
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 794 AA; 86513 MW; A550588D5D0EEDC5 CRC64;
MGKKRIYELA KEINVSSKQL IAKAEEKGFP VKNHMSTLGE NEERQLRAAF KPKAAHQSTQ
ATGHPHRSTT TARGGQSTGK PAQRSTDRAA HASAKPQQKQ AARPAQQNQG QQSNRTTSNA
QHNKNNGQTG AQHGTHNSGT GRFGGSLNNN TNNNNGRRGG SSNGRGGRNN RNNRNNRRRN
NNNNRYKKNQ RIKDTNQHKG APERKNKALP ETLVYTDGMN AQDLAKLLHR SSAEIVKKLF
MLGVMVNQNQ SLDKDTIEIL ASDYGIAAKE KVQVDVSDID KAFDAEMANT KHLVTRAPVV
TIMGHVDHGK TTLLDHLRHS HITAGEAGGI TQAIGAYQVH YNDKLITFLD TPGHAAFTEM
RARGAEITDI TILVVAADDG VMPQTIEAIH HAKAAGTPII VAVNKIDKPG ANPNHVMEQL
TEYELIPEDW GGDTIFVNIS AKFGKNIDEL LDMILLQSEV MELKANPDQN GAGSVIEARL
DQGKGSVATL LVQQGTLHVG DPIVVGNTFG RVRTMTNERG RAIKSAVPAT PVEITGLNDV
PEAGDRFVVF DDEKTARAAG EERAKEALVK ERQNTSHVTL DNLFDSLKEG EMKEVDVIIK
ADVQGSVEAL VGSLKKIEVS GVRVNIIHSA VGAINESDVT LAEASNAIII GFNVRPTPQA
RSQADSDKVD IRLHNVIYNA IDEIEAAMKG MLEPTYEEQV IGQVEVRQIY HASKVGTIAG
GMVTDGKITS DSDVRLIRDG VVIYQGKLGS LKRFKDDVKE VKQGYELGFT IENYNDIKVD
DVVEAYVMKE VPVK
//
