ID A0A0M5KTF8_9MICC Unreviewed; 971 AA.
AC A0A0M5KTF8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=AL755_07285 {ECO:0000313|EMBL:ALE05316.1};
OS Arthrobacter sp. ERGS1:01.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1704044 {ECO:0000313|EMBL:ALE05316.1, ECO:0000313|Proteomes:UP000060433};
RN [1] {ECO:0000313|EMBL:ALE05316.1, ECO:0000313|Proteomes:UP000060433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERGS1:01 {ECO:0000313|EMBL:ALE05316.1,
RC ECO:0000313|Proteomes:UP000060433};
RX PubMed=26415659; DOI=10.1016/j.jbiotec.2015.09.025;
RA Kumar R., Singh D., Swarnkar M.K., Singh A.K., Kumar S.;
RT "Complete genome sequence of Arthrobacter sp. ERGS1:01, a putative novel
RT bacterium with prospective cold active industrial enzymes, isolated from
RT East Rathong glacier in India.";
RL J. Biotechnol. 214:139-140(2015).
RN [2] {ECO:0000313|Proteomes:UP000060433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERGS1:01 {ECO:0000313|Proteomes:UP000060433};
RA Kumar R., Swarnkar M.K., Singh A.K., Singh D.;
RT "Complete Genome Sequencing of Arthrobacter sp. ERGS1:01.";
RL Submitted (AUG-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|HAMAP-Rule:MF_00100,
CC 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00100}.
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DR EMBL; CP012479; ALE05316.1; -; Genomic_DNA.
DR RefSeq; WP_054010430.1; NZ_CP012479.1.
DR AlphaFoldDB; A0A0M5KTF8; -.
DR STRING; 1704044.AL755_07285; -.
DR KEGG; are:AL755_07285; -.
DR PATRIC; fig|1704044.3.peg.683; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000060433; 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; 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 PRINTS; PR00315; ELONGATNFCT.
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|ARBA:ARBA00022490, 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:UP000060433}.
FT DOMAIN 464..635
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 52..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 473..480
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 523..527
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 577..580
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 971 AA; 100462 MW; 4D521CADACD21970 CRC64;
MAKARVHELA KELGITSKEA VTKLQELGEF VRSASSTIEA PVVKKLRDAF PTAPKAAESK
PAPAAPATPA AVKPAAKPAE SAPAAPAPAA PAAPAAVPGP KAAAPAAPAK PAEAAPAAPV
VATPAPAAPA APAAAAPKAA PAAGGPRPGN NPFASSQGMP RSGRSDRGEA RNDNRAPESR
GDAPRTPRPA GAGAGAGAGG PRPGNNPFAT SQGMPRPGAP RSAEAGTGGP RPGGPRPGAP
RPGAPRPAGA AGAGGPRPGA PRPGGPRPTP GMMPNRTERP AAPGRGNDRP GAPGRGRPGA
PGATPGGAPG GAPAGGGFGK GGRGRGGTQG AFGKGGAGRG KQRKSKRAKR QELEQMSAPS
LGGVSVPRGD GSTVVRLRRG SSITDFADKI EANPAALVTV LFHLGEMATA TQSLDEDTFA
LLGEELGYKV QVVSPEDEER ELLSSFDIDF DAELEAEGDE DLEVRPPVVT VMGHVDHGKT
RLLDAIRKSD VVAGEHGGIT QHIGAYQIEH EHEGIERQIT FIDTPGHEAF TAMRARGAKV
TDIAILVVAA DDGVMPQTVE ALNHAQAANV PIVVAVNKID KDGANPEKIR GQLTEYGLVP
EEYGGDTMFV DVSARNNINI EELLEAVLLT ADAALDMRAN PNKDARGIAI EANLDKGRGS
VATVLVQSGT LHVGDTIVAG TAHGRVRAMF DENGEVISEA GPSRPVQVLG LSNVPRAGDT
FFVTGDERTA RQIAEKREAA DRNAALAKRR KRVSLEDFDQ AIIEGKVANL NLILKGDVSG
AVEALEDSLL KIDVGDSVQL RVIHRGVGAI TQNDVNLATV DNAIIIGFNV KPAERVAELA
DREGVDMRFY SVIYGAIDDI ELALKGMLKP EYEEVELGTA EIREVFRSSK FGNIAGSIVR
SGTIRRNSKA RVLRGGKVIG ENLTVDSLKR FKDDATEVRT DFECGIGLGS FNDLQAEDII
QTFEMREKPR V
//
