IF2_VIBC1
ID IF2_VIBC1 Reviewed; 894 AA.
AC A7MZI5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN OrderedLocusNames=VIBHAR_03396;
OS Vibrio campbellii (strain ATCC BAA-1116).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=2902295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1116 / BB120;
RG The Vibrio harveyi Genome Sequencing Project;
RA Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA Wilson R.K.;
RL Submitted (AUG-2007) 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; CP000789; ABU72343.1; -; Genomic_DNA.
DR RefSeq; WP_012128823.1; NC_022269.1.
DR AlphaFoldDB; A7MZI5; -.
DR SMR; A7MZI5; -.
DR EnsemblBacteria; ABU72343; ABU72343; VIBHAR_03396.
DR KEGG; vha:VIBHAR_03396; -.
DR PATRIC; fig|338187.25.peg.2800; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000008152; Chromosome I.
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.
FT CHAIN 1..894
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008370"
FT DOMAIN 393..562
FT /note="tr-type G"
FT REGION 25..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..409
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 427..431
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 448..451
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 502..505
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 538..540
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 33..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 402..409
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 448..452
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 502..505
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 894 AA; 97856 MW; ECEF10F62BEB0780 CRC64;
MTQLTVKALS EEIGTPVDRL MEQLADAGMN KASSDHVSDE EKQKLLSHLK KEHGDKSGES
EPTRLTLQRK TRSTLSVAAG GGKSKDVQVE VRKKRTYVKR STIEDDAKRE AEEAAKREAE
ELAKREAEEQ AKREAAEKAQ READEKAKRE ADAKREAEEK AKRAQADKAK KEMNAKNADA
NTQAKKEADE LKRRQEEEAQ RKAEQEAAKL VEEARKLAEE NEARWSEEET KKKELENSDY
HVTTSRYARE AEDAADRKEE GGARRKKKKP AKEEQSRGGR NQRGGKGRNK GKLAKPTSMQ
HGFDKSATVA KQDVVIGETI VLSELANKMS VKATEVIKVM MKMGAMATIN QVIDQETAQL
VAEEMGHKVV LRKENELEEA VLSDRDTNAE AVPRAPVVTI MGHVDHGKTS TLDYIRRTHV
ASGEAGGITQ HIGAYHVETD NGMITFLDTP GHAAFTAMRA RGAQATDIVV LVVAADDGVM
PQTVEAIQHA KAAGVPLIVA VNKIDKEDAN PDNVKNELAQ YDVIPEEWGG ENMFVHISAK
QGTNIDGLLE AILLQSEVLE LTAVAEGMAS GVVVESRLDK GRGPVATVLV QSGTLNKGDI
VLCGQEYGRV RAMRDELGKE ITEAGPSIPV EILGLSGVPS SGDEATVVRD ERKAREVANY
RAGKFREVKL ARQQKSKLEN MFSNMTAGEV AELNVVLKAD VQGSVEAIAD SLLKLSTDEV
KVSIVGSGVG GITETDAVLA EASNAIILGF NVRADASARR AIEAASVDLR YYSIIYQLID
EVKQAMGGML APEFKQEIIG LAEVRDVFKS PKLGAIAGCM VTEGLIKRNN PIRVLRDNVV
IYEGELESLR RFKDDVQEVK NGYECGIGVK NYNDVRVGDQ IEVFEIVEIK RTLD
