ID   IF2_PARL1               Reviewed;         887 AA.
AC   A7HZ93;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Plav_3628;
OS   Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Parvibaculaceae; Parvibaculum.
OX   NCBI_TaxID=402881;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS-1 / DSM 13023 / NCIMB 13966;
RX   PubMed=22675581; DOI=10.4056/sigs.2215005;
RA   Schleheck D., Weiss M., Pitluck S., Bruce D., Land M.L., Han S.,
RA   Saunders E., Tapia R., Detter C., Brettin T., Han J., Woyke T., Goodwin L.,
RA   Pennacchio L., Nolan M., Cook A.M., Kjelleberg S., Thomas T.;
RT   "Complete genome sequence of Parvibaculum lavamentivorans type strain (DS-
RT   1(T)).";
RL   Stand. Genomic Sci. 5:298-310(2011).
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; CP000774; ABS65226.1; -; Genomic_DNA.
DR   RefSeq; WP_012112487.1; NC_009719.1.
DR   AlphaFoldDB; A7HZ93; -.
DR   SMR; A7HZ93; -.
DR   STRING; 402881.Plav_3628; -.
DR   PRIDE; A7HZ93; -.
DR   EnsemblBacteria; ABS65226; ABS65226; Plav_3628.
DR   KEGG; pla:Plav_3628; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_10_1_5; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000006377; 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; IPR004161; EFTu-like_2.
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; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF11987; IF-2; 1.
DR   Pfam; PF08364; IF2_assoc; 1.
DR   Pfam; PF04760; IF2_N; 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..887
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000335496"
FT   DOMAIN          385..553
FT                   /note="tr-type G"
FT   REGION          1..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          394..401
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          419..423
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          441..444
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          495..498
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          531..533
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..216
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..242
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        249..291
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         394..401
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         441..445
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         495..498
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   887 AA;  95737 MW;  1E9DC525394462CF CRC64;
     MTDQADTSER KPKAAGKTLS LKRTVESGHV RQNFSHGRSK SVVVEKKKKR TLKTSADAAP
     AAAPAAAPAA AEEVAKKPVA APEVKPAAPV EERPAPVAKA APEVKAVPAP APAAAPAVEK
     KPSRSRSGVV LRTLTEEEKN ARAQALDSAR EREGEDRRRA EEEARRFAEE DARREAERAA
     AAARAAEEAS RHTADQSTRT RAAEEAKRRL DDDRPAATPA AARPAKEQAI EEDDDKPKRG
     AGHTPAKAPP ARRSEERRRG KLTITKAFDD ESERQRSLAS MRRRVERERK KHMGIQEAPQ
     KIIREVVIPE VITIQELANR MAERAVDVMK ILMKQGIMLK ITDVIDSDTA QLVAEELGHT
     VKRVAESDVE EGLVGEADIE EAKQARAPVV TVMGHVDHGK TSLLDALRKT DVAAGEAGGI
     TQHIGAYQVN LSSGERITFL DTPGHAAFTS MRARGAKVTD IVVLVVAADD GVMPQTIEAI
     NHAKAAGVPM IVAINKMDKP EADPTRVKNE LLQHEVVVED FGGDVLTVPI SAKTGMGLDK
     LEETILLQAE LLDIRANPDR AAEGIIVEAK LDRGRGPVGT VLVQRGTLKV GDIIVAGAEW
     GRVRALINDR GENVESAGPS VPVEVLGLGG APEAGDVISV VESEGRAREV TAYRQRLQRD
     KRVGTGGRTS LDQMLSQLKE QDKKELPIVV KADVQGSAEA IVQALEKLGT DEVTARVLHV
     GVGGVTESDV TLATASRAPI IGFNVRANTQ ARDAARQAGV EIRYYSVIYD LVDDIKAAMS
     GMLSPELRET FLGNAEILEI FNISKTGKVA GCRVTEGVVR RGSHVRLIRD DVVIHEGKLS
     TLKRFKDEVK EVQSGQECGM AFEGYQDMRK GDVIECFDVE VVQRSLA