IF2_PHOPR
ID IF2_PHOPR Reviewed; 899 AA.
AC Q6LUJ2;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=PBPRA0612;
OS Photobacterium profundum (strain SS9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9;
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(2005).
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; CR378664; CAG19033.1; -; Genomic_DNA.
DR RefSeq; WP_011217382.1; NC_006370.1.
DR AlphaFoldDB; Q6LUJ2; -.
DR SMR; Q6LUJ2; -.
DR STRING; 298386.PBPRA0612; -.
DR EnsemblBacteria; CAG19033; CAG19033; PBPRA0612.
DR KEGG; ppr:PBPRA0612; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000593; Chromosome 1.
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; 2.
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..899
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228225"
FT DOMAIN 398..565
FT /note="tr-type G"
FT REGION 31..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..414
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 432..436
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 453..456
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 507..510
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 543..545
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 59..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 407..414
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 453..457
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 507..510
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 899 AA; 98470 MW; 4BCC72CBC37B6A86 CRC64;
MSEVTVKALA EEVGTPIDRL LQQFSDAGIS KKAEDNVSQT EKQSLLSHLQ KEHGGESTDG
TPTRLTLQRK THSTLSVAGT GGKSKSVQVE VRKKRTFVKR SALEEEQRAA DNAKQEAEET
AQREAENVAK RKEDVRLAEE KAKRDEENKA KRNTEDTVKR EATDKRKAEE KAKRTVAVKQ
AKSETELLQL RREEEAKRKA EEDSQRQLEE ARKMAETNEK NWSATEQNVT ANMEKSDYHV
TTSTHARAAE DEQDRKEETT GTRRKKKPAA KKADDRKGRG GRNQRNQRGG RGKQKPQVNA
PTSMQQGFDK TATVAKSDVV IGETIVVSEL ANKMAVKATE VIKAMMKMGA MVTINQVIDQ
ETAALVAEEM GHKVIFRKEN ELEEALMSDR GETQAVESRA PVVTIMGHVD HGKTSTLDFI
RKAHVASGEA GGITQHIGAY HVEIGNGMIT FLDTPGHAAF TAMRARGAQA TDIVVLVVAA
DDGVMPQTVE AIQHAKAAGV PLIVAVNKID KDGANPDNVK NELAQYDIIP EEWGGENIFV
HISAKQGTNI DGLLEAILLQ SEILELTAVK EGMASGVVIE SRIDKGRGPV ATVLVQSGTL
RKGDIVLCGL EHGRVRAMRD ENGKDIESAG PSIPVEILGL SGVPAAGDEA TVVRDDRKAR
EVALYRQGKF RDVKLARQQK SKLENMFSHM EAGEVAECNV VLKADVQGSI EAIADSLMKL
STDEVKVKVV GSGVGGITET DAVLAAASNA IILGFNVRAD VPARRMIENE NLDLRYYSVI
YQLIDEVKAA MGGMLAPEFR QEIIGLAEVR DVFKSPKIGA IAGCMVTEGT IKRNNPIRVL
RDNVVIYEGE LESLRRFKDD TNEVKNGYEC GIGVKNYNDV RVGDQIEVFE IIEIQRTLD
