IF2_BEUC1
ID IF2_BEUC1 Reviewed; 956 AA.
AC C5BWS3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Bcav_2489;
OS Beutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432).
OC Bacteria; Actinobacteria; Micrococcales; Beutenbergiaceae; Beutenbergia.
OX NCBI_TaxID=471853;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-8 / DSM 12333 / NBRC 16432;
RX PubMed=21304633; DOI=10.4056/sigs.1162;
RA Land M., Pukall R., Abt B., Goker M., Rohde M., Glavina Del Rio T.,
RA Tice H., Copeland A., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Hauser L., Chang Y.J., Jefferies C.C.,
RA Saunders E., Brettin T., Detter J.C., Han C., Chain P., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Beutenbergia cavernae type strain (HKI
RT 0122).";
RL Stand. Genomic Sci. 1:21-28(2009).
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:0000255|HAMAP-Rule:MF_00100}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00100}.
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DR EMBL; CP001618; ACQ80739.1; -; Genomic_DNA.
DR RefSeq; WP_015882979.1; NC_012669.1.
DR AlphaFoldDB; C5BWS3; -.
DR SMR; C5BWS3; -.
DR STRING; 471853.Bcav_2489; -.
DR EnsemblBacteria; ACQ80739; ACQ80739; Bcav_2489.
DR KEGG; bcv:Bcav_2489; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_1_11; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000007962; Chromosome.
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; cd03702; IF2_mtIF2_II; 1.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR43381; PTHR43381; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 2.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00487; IF-2; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..956
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000202764"
FT DOMAIN 448..619
FT /note="tr-type G"
FT REGION 50..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..464
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 482..486
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 507..510
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 561..564
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 597..599
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 66..118
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 457..464
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 507..511
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 561..564
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 956 AA; 98104 MW; 33FBB1EEA1CA94E3 CRC64;
MAKVRVHELA RELGVDSKTV LAKLNELGEF VKSASSTIEA PVVRRLRESF PADSGGAANG
APAAPKPARA PKPAPKAAPA PPVEEAPAEP APPAAPEVVA APEAPVAAPE PPAPSREAEV
PEAPAAERPA AQARPATPGP RPAPRAAEKP ADTRTPRPGN NPFASSQGMP RPGGQGGPRP
GGPRPSGGGG PRPGNNPFAP SQGMPRPGGS GAAGPRPGGT GAAGPRPGGS GQGGSRPSPG
MMPGRSAVGR PGAPARGGSG GPGGGRGGPG GGRGGGGGFG GAPGRGGPGG APGGGGGFSG
GGRSGRGGRG GTQGAFGRAG GKPVRARKSR RAKRQEFEQM SAPSIGGVQV PRGDGTTVVR
IRRGASLSDF ADRIDANPAS LVTVLFHLGE MATVTQALDA GTFEALGAEL GYVIEIVSPE
DEERELLGSF DIDLDAEAAA ESDEDLEARP PVVTVMGHVD HGKTRLLDAI RSTDVVAGEA
GGITQHIGAY QVHVTHEDAD RAVTFLDTPG HEAFTAMRAR GADVTDIAIL VVAADDGVMP
QTIEALNHAQ AANVPIVVAV NKVDKEGANP DKVMQQLTEY NLVAEAYGGD TMFVNVSAKN
GTGIDELLEA VLLTADAALD LRANPNKDAR GVAIEANLDK GRGAVATVLV QSGTLTVGDS
IVAGTAYGRV RAMFDENGDN LSEATPSRPV QVLGLTSVPR AGDSFLVAPD DRTARQIADK
RDAAERAATL AKRRKRISLE DFTQALEQGK VSTLNLVLKG DVSGAVEALE DALLQLDVGA
EVDLRIIHRG VGGITQNDVN LATVDNAIII GFNVRPDVRV AELADREGVD IRYYSVIYAA
IEDVENSLKG MLKPEFEEVQ LGTAEVLQVF RSSKFGNIAG SRVRSGLIRR GASARVLRDS
VVIGDNLSIG SLRREKDDVT EVRDGFECGI GLGSFNDLRE GDVIETFEVR EKERAS
