IF2_DESAH
ID IF2_DESAH Reviewed; 1024 AA.
AC C0QHM2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=HRM2_04660;
OS Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS HRM2) (Desulfobacterium autotrophicum).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulforapulum.
OX NCBI_TaxID=177437;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43914 / DSM 3382 / VKM B-1955 / HRM2;
RX PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA Meyerdierks A., Gottschalk G., Amann R.;
RT "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT reducer oxidizing organic carbon completely to carbon dioxide.";
RL Environ. Microbiol. 11:1038-1055(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; CP001087; ACN13580.1; -; Genomic_DNA.
DR RefSeq; WP_012662829.1; NC_012108.1.
DR AlphaFoldDB; C0QHM2; -.
DR SMR; C0QHM2; -.
DR STRING; 177437.HRM2_04660; -.
DR EnsemblBacteria; ACN13580; ACN13580; HRM2_04660.
DR KEGG; dat:HRM2_04660; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_7; -.
DR OMA; VAMSKID; -.
DR OrthoDB; 57705at2; -.
DR Proteomes; UP000000442; 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..1024
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000202769"
FT DOMAIN 518..687
FT /note="tr-type G"
FT REGION 33..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..534
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 552..556
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 573..576
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 627..630
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 663..665
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 34..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 527..534
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 573..577
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 627..630
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1024 AA; 111558 MW; 5E5EBAC36919A416 CRC64;
MAKIRVYELA KKLNMTNKAL LTKLKAMNIE AKSHMSSLED DTEARVRESL HGMKNKQADT
RVKSSVIRRR RPPKPEPSVT ELPDDEAAGS NGAAEEKITT PGPVTGDEMT ETSTPAPVKS
KIPLKAQTDS TNRPTPEDPV VKATELKPKK VTKPKSSPAR VILRPDTPAK EEPTKAKEVP
AAKEVPAAKE APKVKETSKA VNVSEDEVNP LPTKNVELNS GDSKPDGALE EKSETDEKAL
EKEPTIKQED TILEDNHARK EVRSVAVDDD DKNLDTAEAK DKKRKKKKVQ KRSEPAKIIK
MAVPISVRSR NKVKTEATQA PTSPQRPKVH PKPADKGPAR AQAHRPDTGR DAVVLPGEGD
GEVKRSKKKE WKKKGVGGPG VEFAPKGAPR KRKSVVEGKD LYEKGRSGKK GRRKDGRVKK
TKTMKTQITV PKAIKRRIKI DEVIELSELA KRMGIKANEM IVKLMGMGVM ATVNQTIDFD
TACLVAAEFD YEVEKASVEE DIVLQVQEAE IDPDKLVSRP PVVTIMGHVD HGKTSLLDVI
RKSKVATGEA GGITQHIGAY RVKTKKGTIT FLDTPGHAAF TSMRSRGAQV TDLVVLVVAA
DDGVMPQTIE AINHSKAANV PVVVAVNKMD KPGADPDKVM RELSEHGLLA EDWGGDVIFA
KVSAKTGKGI DGLLEMILLQ SEVLELKANP DSPATGHVVE ARLDAGRGPV ATILVNQGTL
KAGQPVVCGL YSGKIRVMID DMGDDVEFAG PSTPVEIVGL SGVPEAGDEF VALDSEKDAK
QVSDSRMQKQ RAKVLAKRSR ANLEKLFESM GADEIKELKL IIKADVHGSL EALNDSIMKL
AQDEVDITIV HSGTGAINES DVSLAAVSDA IIIGFNVRPT PKVRSMAKDE NVDMRFYDII
YNVINDIKAA ITGLMPSTFH EVIIGRAEVR DTFVIPHKGL TIGGSFVLEG KIARGFKVRL
LRDGVVKCDS TLSSLRRFKD DVKEVAHGYE CGIGIERYND IKIGDIFECY EIEERKAQVE
QIKE
