ID A0A0R1Y3V3_9LACO Unreviewed; 904 AA.
AC A0A0R1Y3V3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=FC83_GL002251 {ECO:0000313|EMBL:KRM36847.1};
OS Agrilactobacillus composti DSM 18527 = JCM 14202.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Agrilactobacillus.
OX NCBI_TaxID=1423734 {ECO:0000313|EMBL:KRM36847.1, ECO:0000313|Proteomes:UP000051236};
RN [1] {ECO:0000313|EMBL:KRM36847.1, ECO:0000313|Proteomes:UP000051236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18527 {ECO:0000313|EMBL:KRM36847.1,
RC ECO:0000313|Proteomes:UP000051236};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRM36847.1}.
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; AZGA01000001; KRM36847.1; -; Genomic_DNA.
DR RefSeq; WP_057002234.1; NZ_AZGA01000001.1.
DR AlphaFoldDB; A0A0R1Y3V3; -.
DR STRING; 1423734.FC83_GL002251; -.
DR PATRIC; fig|1423734.3.peg.2275; -.
DR eggNOG; COG0532; Bacteria.
DR Proteomes; UP000051236; 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:UP000051236}.
FT DOMAIN 405..574
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 38..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..556
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 54..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 414..421
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 460..464
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 514..517
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 904 AA; 99427 MW; B802A4D7EAD2B92A CRC64;
MGKKRIYEFA KELNLPSKEV VEAAQKAGLD IKNHMSSVEV GQEQKIKQAL HVDTGVTSGA
SKAGSQQPRA AQPRPAHQHT PARPSSHQNR AVTRNTAAAS QPSNPNQNNN SHHTTNSNSN
HTGTTQQNNR PRQDNNRMQS SQQKSNNGTS QTNNRPNNRN SRPQNQNRNA STNAGQNRTN
NNQGQNRNAI NNQNRSNNNQ NRNTSNPQNR TNTTTNNRTN NNRPASNNAR PQNSRLQNSG
STTNQTRTTG NTQNRTGQRT TTGGNTGGGY NNRNSNNRGG SWSNNRGGNA FNRRRNNKKN
RRRDTTPKKP MPQRKDRPLP SVLVYTEGMN AQDLGKILHR EPAEIVKKLF MLGVMTNQNQ
SLTKDAIELL ATDYGIDAKE KVEEDITDLD KIFNDEEQND AHLESRPPVV TIMGHVDHGK
TTLLDKLRHT HVTASEAGGI TQHIGAYQVK LDNRVITFLD TPGHAAFTNM RARGADVTDI
IILVVAADDG VMPQTIEAIN HAKAAKAPII VAVNKIDKPG ANPNHVMEQL TEYGLIPESW
GGDTIFVEIS AKFGKNIDEL LEMVLLEADM LELKANPQQR GVGTVLEARL DKGKGPVASL
LVQQGTLHVG DPIVVGNTFG RIRVMTNDRG RRVKEALPSE PVEITGLNDV PDAADKFAVY
EDEKTARAAG EERAKKALLE ERSHTTHVTL DNLFESMKQG ELKEVDVIIK GDVQGSVEAL
ANSLQKIEVA GVRVNIIHQA VGAINESDVT LAAASQAIIL GFNVRPTANA RSQADMDDVD
IRLYNVIYNA IEEVESAMKG MLEPTYQEKV TGNLTVRETY KVSKVGTIAG AYVNTGYITR
DSGVRLIRNS IVIFEGKLAS LKRFKDDVKE VRSGFDCGLT IENYNDIKVD DEIEAYVMEE
VPVK
//
