IF2_CHRSD
ID IF2_CHRSD Reviewed; 843 AA.
AC Q1QSZ0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Csal_3074;
OS Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 /
OS NCIMB 13768 / 1H11).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Chromohalobacter.
OX NCBI_TaxID=290398;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11;
RX PubMed=22675587; DOI=10.4056/sigs.2285059;
RA Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D.,
RA Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T.,
RA Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C.,
RA Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.;
RT "Complete genome sequence of the halophilic and highly halotolerant
RT Chromohalobacter salexigens type strain (1H11(T)).";
RL Stand. Genomic Sci. 5:379-388(2011).
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; CP000285; ABE60418.1; -; Genomic_DNA.
DR RefSeq; WP_011508364.1; NC_007963.1.
DR AlphaFoldDB; Q1QSZ0; -.
DR SMR; Q1QSZ0; -.
DR STRING; 290398.Csal_3074; -.
DR PRIDE; Q1QSZ0; -.
DR EnsemblBacteria; ABE60418; ABE60418; Csal_3074.
DR KEGG; csa:Csal_3074; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_1_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000239; 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; Reference proteome.
FT CHAIN 1..843
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008226"
FT DOMAIN 343..512
FT /note="tr-type G"
FT REGION 26..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..359
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 377..381
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 398..401
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 452..455
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 488..490
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 33..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..240
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 352..359
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 398..402
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 452..455
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 843 AA; 91352 MW; 0CBD020232CAA7F8 CRC64;
MSDMTVKDFA SKVGRDVSRL LEQMQEAGLP HKTEGDAVSE EDKQRLLEHL TRSHGGDSGA
TKNRVTLTRN TKSRIRSGDG RGKAIDVQVR KKRTYVKREP EPAEEKAAEE TGPRQLVGDM
ASANQAKADE AAKAEQAAAE QAAKAKAEEE AAAAAASKAA ESEPVAEAPG APQPEEPETA
SEPFVEAPPK EPRTPNRRGQ NHQKKDTGRG RKRDDDEERR ERGERRRGNA KKTKRSERRG
SRRGGGRDNQ HGFQKPTQPI VREVAIPESI SVADLADKMS IKANEVIKAM FTMGAAVTIN
QTIDQDTAAI VVEEMGHKPK LVKDDALETE VLEGISYEGE EITRAPVVTV MGHVDHGKTS
LLDYIRRTKV ATGEAGGITQ HIGAYHVEHE SGDITFLDTP GHAAFTAMRA RGAQATDVVI
LVVAADDGVM PQTVEAVEHA KAAGVPLVVA VNKIDKEGAD PDRVKNELSQ YGVISEAWGG
DTQFVHVSAK SGEGIDALLE AILLVSEVLE LKAVPEAPAK GVVVESQLDK GRGPVATVLV
QNGTLKRGDI VLAGLHYGRV RALVNELGKR VEEVGPAMPV EIQGLDGTPE AGDEFIVVAD
EKKAREVANF RQGKYREVRL ARQQKAKLEN MFSQMGQDEV AKVNIVLKAD VQGSLEAIRG
ALEELSTDEV KVAVVSSGVG GITGTDANLA VASEAILVGF NVRADVSARE IVEREGLDLR
YYSVIYQLID EVKQAMSGML APEWKEEIVG VAEVRDVFKA PKIGAVAGCM VVEGTVYRHK
RIRVLRENVV IYEGELESLR RYKDDIGEVR SGMECGIGVK NYNDVQVGDK IEVFDQVKVE
RSL
