IF2_ALKMQ
ID IF2_ALKMQ Reviewed; 706 AA.
AC A6TRK7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Amet_2673;
OS Alkaliphilus metalliredigens (strain QYMF).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=293826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QYMF;
RX PubMed=27811105; DOI=10.1128/genomea.01226-16;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA Richardson P., Fields M.W.;
RT "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT leachate ponds.";
RL Genome Announc. 4:0-0(2016).
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; CP000724; ABR48825.1; -; Genomic_DNA.
DR AlphaFoldDB; A6TRK7; -.
DR SMR; A6TRK7; -.
DR STRING; 293826.Amet_2673; -.
DR EnsemblBacteria; ABR48825; ABR48825; Amet_2673.
DR KEGG; amt:Amet_2673; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000001572; 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; 2.
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..706
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000057648"
FT DOMAIN 208..375
FT /note="tr-type G"
FT REGION 55..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..224
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 242..246
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 263..266
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 317..320
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 353..355
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 55..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 217..224
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 263..267
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 317..320
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 706 AA; 76793 MW; 3678BE25D517B0F2 CRC64;
MSKVRVYQLA KELGVSSKEL IIKLKDLSIE VGNHMSTLND DDANLLIELF TEDNKEVNSD
SNQESKVNTD DKLDKIDKPN KIENAPSEEN PKKNKKSKKK QKNKKKGPTM KDEKGLIEEN
TDEQILEIGE SIILKDLTHM LDKTPTEVIT KLIGLGMMVT INQEIDFDTA AMVASEYGVE
LKQAGVMDDS DVVDDLIIPE DDEKDLMSRP PVVTVMGHVD HGKTSLLDAI RKTKVTAKEA
GGITQHIGAS EIQINDKKIV FLDTPGHEAF TSMRARGAKV TDIAILVVAA DDGVMPQTIE
AINHAKAAEV PIIVAINKID KPGANQDRVK QELSDHGILI EAWGGDVIAV PVSAIEGTNI
NELLEMILLV SEVEEFKANP NRQAIGVVIE AKLDKGKGTV ATVLIQNGTL HVGDSVVVGS
TYGRIRAMTN HVGEKLREAT PSTAVEITGL SDVPEAGNQL VVVADDKMAR NTAEKRAHKA
KVAQQKITQR VSLDDLYNQM QQGEIKELNI IVKADVQGSV QAVKQSLEKL SNDKVSLRTI
HGGVGAITES DVMLAAASNA IITGFNVRPT STATAISKKE KVDIRTYRII YNAIEDIEAA
MVGMLDPEFK EVDLGKAEVR AAFKVPGAGV VAGSYITEGK ILRSASIRLV RDGIVVHEGA
IGSLRRFKDD VKEVNTGYEC GIGIDKFNDV KEGDIIEAYT MEEIKR
