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   27-MAR-2024, entry version 124.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN   OrderedLocusNames=Psyc_0069;
OS   Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4).
OC   Bacteria; Pseudomonadota; 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   KEGG; par:Psyc_0069; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_6_3_6; -.
DR   OrthoDB; 9811804at2; -.
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; cd01887; IF2_eIF5B; 1.
DR   CDD; cd03702; IF2_mtIF2_II; 1.
DR   CDD; cd03692; mtIF2_IVc; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.30.56.50; Putative DNA-binding domain, N-terminal subdomain of bacterial translation initiation factor IF2; 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; 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   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; PF08364; IF2_assoc; 1.
DR   Pfam; PF04760; IF2_N; 1.
DR   SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF46955; Putative DNA-binding domain; 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; 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
//