IF2_METPB
ID IF2_METPB Reviewed; 990 AA.
AC B1ZDQ8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Mpop_2819;
OS Methylorubrum populi (strain ATCC BAA-705 / NCIMB 13946 / BJ001)
OS (Methylobacterium populi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=441620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-705 / NCIMB 13946 / BJ001;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Marx C., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium populi BJ001.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001029; ACB80974.1; -; Genomic_DNA.
DR RefSeq; WP_012454696.1; NC_010725.1.
DR AlphaFoldDB; B1ZDQ8; -.
DR SMR; B1ZDQ8; -.
DR STRING; 441620.Mpop_2819; -.
DR PRIDE; B1ZDQ8; -.
DR EnsemblBacteria; ACB80974; ACB80974; Mpop_2819.
DR KEGG; mpo:Mpop_2819; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_1_5; -.
DR OMA; RDVMMAG; -.
DR Proteomes; UP000007136; 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; 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; 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..990
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093803"
FT DOMAIN 486..656
FT /note="tr-type G"
FT REGION 1..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..502
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 520..524
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 542..545
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 596..599
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 632..634
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..80
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..228
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 495..502
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 542..546
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 596..599
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 990 AA; 106294 MW; 9494F59226502EED CRC64;
MSDTNNPGDK TQTRAPSKPL TLKRPVEQGT VRQSFSHGRS KSVVVETVKR RTIGAAPGTV
APREPVAAPP PRPASVAPAP AAPARPAGRS ASGVVLRTLS EQERDARAAA LADAQRREAE
ARARAEAEVK ARRDREEAER REREAAEARR REEEERRRQE DELRRKAAED SRRRAEEEAA
RAAAAAPVDE APAEAPAAPA PVAEAAPTVA PTPAPAPRPA PAPARPAAAA PAARPGAAPQ
RPAASGARPG VAGARPAPTA ARPAAPQAPA EPRRTITADV KKPRDLNFMA RPAPAPEPEK
APSPTTAARP AGTAARPAAR PGAAAAEDES DTKRVIRRPG MPLKIITPPK TPKSPGGDRN
RGRLTIANAT AGEDERTRSV ASFRRRQQRM SGHRHEEPKE KIARDVTIPE TITIQELANR
MSERAVDVIR LLMKQGQIHK ITDVIDSDTA QLIAEEMGHT VRRVAESDVE EGLTSDEPDL
EEDLEPRPPV VTIMGHVDHG KTSLLDAIRR ANVVEGEAGG ITQHIGAYQV AAPSGDLITF
IDTPGHAAFT SMRARGAKVT DIVVIVVAAD DGVMPQTIEA IQHAKAAGVP MIIAINKIDK
ADANPQRVRT ELLQHDIQVE SMGGETLEFE VSAKTGDGLP ELLEGLQLQA EIMNLRANEK
RDGEGTVIEA QLDRGRGPVA TVLVQRGTLF TGDIIVAGAE WGRIRALIDD TGKHIPYAGP
SVPVEVLGFN GTPDAGDRVI VVPNEARARE VTEYRARIKR ERLNARTGGA NRSLVDMMRE
AKEGANRKEL PIIIKGDVQG SVEAINGALT ALGNDEVGVR ILLSGVGGIT ESDITLANAS
KAVVIGFNVR AHKEARNAAE RDGTEIRYYS IIYDLVDDIK ATLSGMLPPT LREERLGEAQ
ILQIFDVSKV GKIAGCRVME GVVQRGAHVR LLRNDVVIHE GKLAQLKRLK DDAKEVTAGY
ECGMSFQNYQ DMRVGDFIEC FNVEEIKRTL
