IF2_PSYA2
ID IF2_PSYA2 Reviewed; 908 AA.
AC Q4FVL5;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Psyc_0069;
OS Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=259536;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17307 / VKM B-2377 / 273-4;
RX PubMed=20154119; DOI=10.1128/aem.02101-09;
RA Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N.,
RA Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C.,
RA Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P.,
RA Murray A., Thomashow M., Tiedje J.M.;
RT "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive
RT Siberian permafrost bacterium, reveals mechanisms for adaptation to low-
RT temperature growth.";
RL Appl. Environ. Microbiol. 76:2304-2312(2010).
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; CP000082; AAZ17943.1; -; Genomic_DNA.
DR RefSeq; WP_011279382.1; NC_007204.1.
DR AlphaFoldDB; Q4FVL5; -.
DR SMR; Q4FVL5; -.
DR STRING; 259536.Psyc_0069; -.
DR EnsemblBacteria; AAZ17943; AAZ17943; Psyc_0069.
DR KEGG; par:Psyc_0069; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000546; 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; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR013575; IF2_assoc_dom_bac.
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; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 1.
DR SUPFAM; SSF46955; SSF46955; 1.
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..908
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228233"
FT DOMAIN 409..578
FT /note="tr-type G"
FT REGION 52..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..425
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 443..447
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 464..467
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 518..521
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 554..556
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 67..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 418..425
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 464..468
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 518..521
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 908 AA; 99875 MW; 7B5B55166A0CB41C CRC64;
MADKTVKELA DMVSKTASAV QQQLVDAGLP ARAEGDLVTE LEQEKLVTYL KQSHGQEEKR
RISLKSKTTS TARVTGSSGK SKSVNVEVRK KKVFEKPDPE KMAEELAARE QAMIESQARA
AKDAEDRAAT KKKSEERQAA TLAAMRASLG SSKKSDDKND DISTSVVVKK GGKTTIEVKP
KEQPKKKVAA TKPKVETAVE RKAREVREKE EARLREIETE TRRTQAEEAQ KRTLEQMRKM
AGQYTDQPAT EVRKDEPLAE GLVGDALEES FEKERREIKR GTSSTTARGR GRRKNQDERE
IKNRKNGLRS SQSAQHKFEK PVEKIVYDVE ISEQITVSDL AQRMAVKARE VTKLLMKMGE
IARESDTIDQ ATASLIVEEM GHNPVPVSDT KVEDDLQDAA DERSSNVQTR PPVVTIMGHV
DHGKTSLLDK IRETKVATGE AGGITQHIGA YHVKTARGVI TFLDTPGHAA FSAMRSRGAQ
ATDIVVLVVA ADDGMMPQTE EAIDHARAAG TPLIVAINKM DKPSADPDRV LNELTAKEVV
SEEWGGDTPM ARISAKTGDG IDELLELISL QAELMELEAP LDGPAQGVVI ESRLEKGRGP
VVSVLVKKGT LKQGDLVLAG EHYGKVRAMT DEHGQRIQSA GPSIPVEILG LPETPAAGSE
FLVLTDEKKA REVADFRTNR ERERQLERQN AMRLESMFDQ MEQGNVSYLN IVLKTDVRGS
LEALLSALNE LSTDEVKVRV ISSGVGPISE SDVTLAESSE AVLLGFNVRA DATARRKSDT
ANMDIRYYSV IYGLIDDVKA AMSGMLAPEH REKILGVADV REVFRSSKFG AAAGCMVVEG
TIYRNKPIRV LRNDQVIFTG QLQSLRRYKE DVNEVRTGME CGLAVRGYDV EAGDKIEVFE
IQEFARTI
