ID A0A0R2L687_9LACO Unreviewed; 958 AA.
AC A0A0R2L687;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=IV55_GL002009 {ECO:0000313|EMBL:KRN95366.1}, LSI01_04560
GN {ECO:0000313|EMBL:GEK28145.1};
OS Furfurilactobacillus siliginis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Furfurilactobacillus.
OX NCBI_TaxID=348151 {ECO:0000313|EMBL:KRN95366.1, ECO:0000313|Proteomes:UP000051139};
RN [1] {ECO:0000313|EMBL:KRN95366.1, ECO:0000313|Proteomes:UP000051139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22696 {ECO:0000313|EMBL:KRN95366.1,
RC ECO:0000313|Proteomes:UP000051139};
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).
RN [2] {ECO:0000313|EMBL:GEK28145.1, ECO:0000313|Proteomes:UP000321429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101315 {ECO:0000313|EMBL:GEK28145.1,
RC ECO:0000313|Proteomes:UP000321429};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Lactobacillus siliginis NBRC 101315.";
RL Submitted (JUL-2019) 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:KRN95366.1}.
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DR EMBL; BJUD01000005; GEK28145.1; -; Genomic_DNA.
DR EMBL; JQCB01000009; KRN95366.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2L687; -.
DR STRING; 348151.IV55_GL002009; -.
DR PATRIC; fig|348151.3.peg.2062; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000051139; Unassembled WGS sequence.
DR Proteomes; UP000321429; 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}; Reference proteome {ECO:0000313|Proteomes:UP000051139}.
FT DOMAIN 459..628
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 38..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..610
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 111..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 468..475
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 514..518
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 568..571
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 958 AA; 103312 MW; F9C6C1C391544382 CRC64;
MANKRIYELA KELNVSSKDL LATANAKGMN FSNHMATVSD TQEQQLRGKA APKKAAATTE
KTTTPTTTDA EPAKRKVVHH LINHNKKPDH RHTNFGRNGG ANLHGEGRIM NLNNPRSNNR
PAKQQRSEAQ SSAPKSAAAQ QSAAATSQAA SVAPKSAATS ASKVTSTAAS QAPKTATNLA
PRSTNNNRPA ASHNNSTSRP ASSTNNRSTS SNGNRSNNNG SRNTTSSTNR SNGGYNSNRS
NGQSSSNNRP NNGGNRSTSQ NRGTSQNSRN NTSSRPSNNS SRPTNTNSRP SSSNNSSRSS
QPSTTGSTNN RGGNTNNNRF GPNATSSRGR GGNRRGGQQQ YGQKHQKRNK RNQRIKQTTQ
AVPAPTRKDR PLPEVLMYTV GMNAQDLGKI LHREPTEIIK KLFMLGVMVN QNQSLDKDTI
EVLAADYGIN AEEKPQEDIA DIDKFFEEQA QTDPTKLVAR PPVVTIMGHV DHGKTTLLDQ
LRNSHITAGE AGGITQKIGA YQVELKDRKI TFIDTPGHAA FTAMRARGAD ITDITILVVA
ADDGVMPQTI EAIHHAQAAK TPIIVAVNKI DKPGANPNHV IEQLAEYNLI PEAWGGETIF
VEISAKFDKN LDELLDMVLL QADLMELKAD PDQRALGSVI EARLDKGRGP VATVLVQEGT
LRIGDPIVIG NTYGRIRTMN NDRGQDVKEA TPATPVEITG MNDVPEAGDK FVVFADEKSA
RAAGEERASR ALVEERSHGN HVTLDNLFDT MKEGEMKEVD VIIKADVQGS VEALANSFQK
IQVDGVRVNI IHKAVGAINE SDVTLAEASD AIIVGFNVRP TVQAKSQADG DGVDIRLHNV
IYNAIDEIES AMKGMLEPVY EEQVTGQVEV RELYKVSKVG TVVGGLVTEG YISSDAGIRL
IRDGVVIYEG KLGSLQRFKD QVKQVKAGFD LGLTIAGYND IKEGDVIEAY VMKEVPVE
//
