ID IF2_MAGMM Reviewed; 949 AA.
AC A0LE19;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Mmc1_3727;
OS Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Magnetococcales;
OC Magnetococcaceae; Magnetococcus.
OX NCBI_TaxID=156889;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1;
RX PubMed=19465526; DOI=10.1128/aem.02874-08;
RA Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT coccus strain MC-1.";
RL Appl. Environ. Microbiol. 75:4835-4852(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; CP000471; ABK46212.1; -; Genomic_DNA.
DR RefSeq; WP_011715264.1; NC_008576.1.
DR AlphaFoldDB; A0LE19; -.
DR SMR; A0LE19; -.
DR STRING; 156889.Mmc1_3727; -.
DR KEGG; mgm:Mmc1_3727; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_1_5; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000002586; 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; 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; 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; 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..949
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335489"
FT DOMAIN 445..619
FT /note="tr-type G"
FT REGION 54..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..461
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 479..483
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 501..504
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 555..558
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 591..593
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 54..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 454..461
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 501..505
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 555..558
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 949 AA; 103803 MW; 7AB3990E63835072 CRC64;
MSDNKPSEGD NKLQLKAPRR IVLKKTVEGS SIKQNFAHGR SKSVAVEVRR KKTFLKPGSK
EGGFLIDQEK PEEIEEKKEA PKSPKRGEER HILRPLTPEE IEAKQKELEA KRQAEEEAAR
QKAEQEAARQ KQEAEAARRK AEQEAARQKQ EAEAARRKAE EEAARAAAAA PAAPVAAPAE
AAPAVPVAVA EPVVVAQPAP EAPAPVVEEE MVEAKPLPAA APAAPSAPVR LLHQPVEEEP
KRKLSKAQRE EMARRKTEDL VSKRLNQLEE LREQKRKEDA RKEAEVALAK KEKPVVAATA
AAAAEVVAGR TPREDSAGEP FSAGRRKNKK YQDNEDRLQQ PRGKSRRRKP FKSEMQAPAP
VYREVTIPET ITVGELANRM AVKSSEVIKL LFAQGMLVTI NQTLDQDTAV LVVEEMGHKP
KSVSESAAIE AELDAGEDAA EDMETRPPVI TVMGHVDHGK TSLLDAIRST DVTSREHGGI
TQHIGAYQVT LASGDKITFL DTPGHSAFTA MRARGAQVTD IVVLVVAADD GVMPQTVEAI
NHAKSAKVPI VVAVNKIDKP GSNPDRVMQQ LSDHGLVPEA WGGDTIFVHV SAKSGEGIST
LEEMLLLQAE MLNLQSNPTK KRARGTIIEA NLDRGRGAVA TCLVQNGTLR VGDICVVGNE
WCRVRALNDD RGNQVSEASP SMPVEIIGLS GVPQAGDDLV AVNDERRARE IAQFRQQKDK
EAIQAKQQPA TRLEDMFEHI EQGEVEELNV VLKADVQGSV EAVAEALRKI KHEQIEVRVI
HTGVGGINES DVMLAVASGA ITVGFNVRAD AKARDLAKRE QIDLRFYNVI YDLVDDISLA
LEGRLAPTVR EKVLGHAQVR EVFRITKIGN VCGCLVTDGI IQRNGKLRIL RQNVVVYEGP
VSALKRFKDD VKEVREGFEC GISIEKFNDV KVDDVLECYV EEQVKQTLS
//
