IF2_METCA
ID IF2_METCA Reviewed; 868 AA.
AC Q609C0;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=MCA1315;
OS Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylococcus.
OX NCBI_TaxID=243233;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J.,
RA Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L.,
RA Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H.,
RA Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R.,
RA Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.;
RT "Genomic insights into methanotrophy: the complete genome sequence of
RT Methylococcus capsulatus (Bath).";
RL PLoS Biol. 2:1616-1628(2004).
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; AE017282; AAU92656.1; -; Genomic_DNA.
DR RefSeq; WP_010960596.1; NC_002977.6.
DR AlphaFoldDB; Q609C0; -.
DR SMR; Q609C0; -.
DR STRING; 243233.MCA1315; -.
DR PRIDE; Q609C0; -.
DR EnsemblBacteria; AAU92656; AAU92656; MCA1315.
DR KEGG; mca:MCA1315; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000006821; 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..868
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228213"
FT DOMAIN 369..538
FT /note="tr-type G"
FT REGION 103..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..385
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 403..407
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 424..427
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 478..481
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 514..516
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 103..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..211
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 378..385
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 424..428
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 478..481
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 868 AA; 94854 MW; DD15BEB39ED7E8DA CRC64;
MSDVTVRQLA GIVGIPLDRL LHQLGDAGLQ ISDADDVLSD AEKMKLLNHL RQSHGKVQES
VTEPKRVTLQ RRSVTELKQG TVPGKGAKTI SVEVRKKRTY VKRSELPETS DRLSEAEQAR
RALEEQQQRE LAEQEARRQQ EEMLREQAAE EERRRQEEAA RTAEERRRRD EEERQAAAER
ETVAAKPAPV AAPPIPRPAP EPRPPARPSA GKPKAEAPRA HPAERETEAR GDKRSAGLSR
KDEYRELQGD DFRKGGGKRK KPKTGRPMLM PEQKHGFEKP TAPIVYEVAV PESITVSDLA
QRMSVKGVEV IKALMKMGVM ATINQVLDQE TAILVVEEMG HKAIAQKEDD LEAEIMANLA
AEAEAPQLPR PPVVTIMGHV DHGKTSLLDY IRKSRVAAGE AGGITQHIGA YQVKTDHGSI
TFLDTPGHAA FTAMRARGAK VTDIVVLVVA ADDGVMPQTR EAVEHSRAAG VPLVVAMNKM
DKADADPDRV KQELVGLNVV PEEWGGDVQF VPVSAKTGAG IDTLLDAILV QAEVLELKAP
VAIPAAGVVL ESKLEKGRGP VADILIQRGT LKKGDFLLCG KEIGRVRAMF NENGKPLKEA
GPSAPIEVLG LSGAPEAGDE FIVVADERKA REIALHREEK LRSTKLAAQQ AAKLEDVFSL
MGSEETIDLN LVIKADVQGS LEALRSALTE LSTDKVKVRV IGGGVGGISE TDANLALASN
AILIGFNVRA DGSARKLIEE RGIDLHYYSV IYNAIDEVKK SINGMLEPEF KEQIIGIAQV
REVFRSSKFG TVAGCLVVEG HVRRNLPIRV LRDNVVIFEG QLESLRRFKD DVNEVKSGME
CGIAVRNYND VREGDQIEVF EKVQVAPH
