IF2_PECCP
ID IF2_PECCP Reviewed; 899 AA.
AC C6DKK3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=PC1_0585;
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-2009) 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; CP001657; ACT11640.1; -; Genomic_DNA.
DR RefSeq; WP_012773288.1; NC_012917.1.
DR AlphaFoldDB; C6DKK3; -.
DR SMR; C6DKK3; -.
DR STRING; 561230.PC1_0585; -.
DR EnsemblBacteria; ACT11640; ACT11640; PC1_0585.
DR KEGG; pct:PC1_0585; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002736; 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; 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..899
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000202781"
FT DOMAIN 398..567
FT /note="tr-type G"
FT REGION 65..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..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 65..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..294
FT /note="Basic and acidic 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; 98571 MW; 592057F652EDB855 CRC64;
MTDVTVKSLA AEIQTPVDRL IQQFADAGMT KSASDAVTQH EKETLLAHLN RDRGNAQGKL
TLQRKTRSTL NVPSTGGKSK SVQIEVRKTR TYVKRDPIDA QQAEEEEQAR REAEEQAQRA
AEEQAKREAE LREAAEKAKR AADEQAKREA AEKAKRDVAE KEKVTNQQNE NMTKPAQAEK
AKREAEAAEL KRKAEEAARL KVEEEARRIA EEARRMAEEN AGRWEAESAK PEESADYHVT
TSHHAREAED ENDRQVEGER RSRSRAGKVT KQKKGNRQSE SKADREEARA VTRGGKGKRK
PSSLQQSFNK PVQAVNRDVV IGETVTVAEL ANKMAVKGSQ VIKVMMKLGA MATINQVIDQ
ETAQLVAEEM GHKVILRREN ELEEAVMSDR DTGVAAEARA PVVTIMGHVD HGKTSLLDYI
RSTKVAAGEA GGITQHIGAY HVETDNGMIT FLDTPGHAAF TAMRARGAQA TDIVVLVVAA
DDGVMPQTIE AIQHAKAAQV PVVVAVNKID KPEADPDRVK TELSQYGVMP EEWGGESQFV
HVSAKAGTGI DELLDAILLQ AEVLELKAVR SGMANGVVIE SFLDKGRGPV ATVLVREGTL
NKGDIVLCGF EYGRVRAMRD ELGREITSAG PSIPVEILGM SGVPAAGDEA TVVRDEKKAR
EVALYRQGKF REVKLARQQK SKLENMFANM TEGEVSELNI VLKSDVQGSC EAISDSLQKL
STDEVKVKIV GSGVGGITET DATLAAASNA IILGFNVRAD ASARRIVESE SLDLRYYSVI
YDLLDEVKQA MSGMLAPEYK QEIIGLAEVR DVFKSPKFGA IAGCMVTEGI VKRHNKIRVL
RDNVVIYEGE LESLRRFKDD VNEVRNGMEC GIGVKNYNDV RPGDMIEVFE TIEIKRTIA
