ID G4T3D5_META2 Unreviewed; 869 AA.
AC G4T3D5;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000256|HAMAP-Rule:MF_00100,
GN ECO:0000313|EMBL:CCE22627.1};
GN OrderedLocusNames=MEALZ_0933 {ECO:0000313|EMBL:CCE22627.1};
OS Methylotuvimicrobium alcaliphilum (strain DSM 19304 / NCIMB 14124 / VKM
OS B-2133 / 20Z) (Methylomicrobium alcaliphilum).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylotuvimicrobium.
OX NCBI_TaxID=1091494 {ECO:0000313|EMBL:CCE22627.1, ECO:0000313|Proteomes:UP000008315};
RN [1] {ECO:0000313|Proteomes:UP000008315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z
RC {ECO:0000313|Proteomes:UP000008315};
RX PubMed=22207753; DOI=10.1128/JB.06392-11;
RA Vuilleumier S., Khmelenina V.N., Bringel F., Reshetnikov A.S., Lajus A.,
RA Mangenot S., Rouy Z., Op den Camp H.J., Jetten M.S., Dispirito A.A.,
RA Dunfield P., Klotz M.G., Semrau J.D., Stein L.Y., Barbe V., Medigue C.,
RA Trotsenko Y.A., Kalyuzhnaya M.G.;
RT "Genome sequence of the haloalkaliphilic methanotrophic bacterium
RT Methylomicrobium alcaliphilum 20Z.";
RL J. Bacteriol. 194:551-552(2012).
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:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000644}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000645}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000256|ARBA:ARBA00007733, ECO:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000644}.
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DR EMBL; FO082060; CCE22627.1; -; Genomic_DNA.
DR RefSeq; WP_014147428.1; NC_016112.1.
DR AlphaFoldDB; G4T3D5; -.
DR STRING; 1091494.MEALZ_0933; -.
DR KEGG; mah:MEALZ_0933; -.
DR PATRIC; fig|271065.3.peg.954; -.
DR HOGENOM; CLU_006301_6_0_6; -.
DR Proteomes; UP000008315; 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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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; 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 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; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 2.
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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00100};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00100}; Reference proteome {ECO:0000313|Proteomes:UP000008315}.
FT DOMAIN 369..536
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 106..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..520
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 106..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..250
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:0000256|HAMAP-Rule:MF_00100"
FT BINDING 424..428
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 478..481
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 869 AA; 94911 MW; FF9BF2EA43BF04A0 CRC64;
MSDKTVRQLA EVVGIPLERL LEQLKEAGLS AHAPDDVISE DEKVKLLAHL RKRHGKSTGE
TDAAPKRVTL KRRTVSELKQ SNAPGSSAKT ISIEVRKKKT YVKRAEVAPV GDEPKESEEI
KKTEERIQAE PTPVSTEQPP VSAVTEEKAT KGEEELFERE QPVDEVATTA EAPQDKISVD
DSEPVDKEAL TEAQAIEIRK ETERKARLSE TERKKEEEKK RRLEAAVEKN AEKVRQLAAA
RMESQKKKRQ GGQAAGKGKK KGKQKDRSGA QADLKHQFEK PVAPVIRDVT IPEHIIVSDL
AQKMSVKAAE VIKQLMKMGM MATINQSIDQ ETAVLLVEEM GHKAIMQSDD DLEAEILAAL
KEESSQEMSR APIVTIMGHV DHGKTSLLDY IRETRVAAGE AGGITQHIGA YQVVTDHGSV
TFLDTPGHAA FTAMRARGAE LTDVVIVVVA ADDGVMPQTK EAVEHARAAN VPIIVAINKI
DKPQANPEKV MQEMSTINVV PEEWGGDVQF IKVSAKTGEG IDDLIEALIL QAEILELKAP
AEGSASGIVV ESRLDKGRGA VATILVQRGM LEKGQFVLCG HEYGRVRAMF NENGKAVKEA
GPSTPVEILG LSGTPNAGDE FLVVQNERAA RELAEHREDK SKISRMAAQQ AAKLDQVFSK
MATGETASLN LVIKTDVQGS LEALRESLIK LSSDEVEVKV VYGGVGGINE GDVNLALASG
AILIGFNVRA DTAARKLIEE KDVDLHYYSV IYQAIDEVKS SISGMLAPEI KETIVGLAEV
RDVFRSPKFG AVAGCMVVEG FVKRNLPIRV LRENVVIYEG QLESLRRFKD DVAEVKMGME
CGIGVKNYND VKVGDHIEVF ERVEVKREL
//
