HIGB_SHIFL
ID HIGB_SHIFL Reviewed; 104 AA.
AC P64580; P42595;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=mRNA interferase HigB;
DE EC=3.1.-.-;
DE AltName: Full=Endoribonuclease HigB;
DE AltName: Full=Toxin HigB;
GN Name=higB; OrderedLocusNames=SF3123, S3330;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. A
CC probable translation-dependent mRNA interferase.
CC {ECO:0000250|UniProtKB:P64578}.
CC -!- SUBUNIT: Probably forms a complex with the antitoxin HigA which
CC inhibits the mRNA interferase activity. {ECO:0000250|UniProtKB:P64578}.
CC -!- SIMILARITY: Belongs to the HigB mRNA interferase family. {ECO:0000305}.
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DR EMBL; AE005674; AAN44595.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP18408.1; -; Genomic_DNA.
DR RefSeq; NP_708888.2; NC_004337.2.
DR RefSeq; WP_000550189.1; NZ_WPGW01000031.1.
DR PDB; 5YCL; X-ray; 3.10 A; B/D=1-99.
DR PDBsum; 5YCL; -.
DR AlphaFoldDB; P64580; -.
DR SMR; P64580; -.
DR STRING; 198214.SF3123; -.
DR EnsemblBacteria; AAN44595; AAN44595; SF3123.
DR EnsemblBacteria; AAP18408; AAP18408; S3330.
DR GeneID; 1026710; -.
DR GeneID; 66506933; -.
DR KEGG; sfl:SF3123; -.
DR KEGG; sfx:S3330; -.
DR PATRIC; fig|198214.7.peg.3710; -.
DR HOGENOM; CLU_153067_0_1_6; -.
DR OMA; VMFFADF; -.
DR OrthoDB; 2072230at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0110001; C:toxin-antitoxin complex; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR InterPro; IPR018669; Toxin_HigB.
DR Pfam; PF09907; HigB_toxin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endonuclease; Hydrolase; Nuclease; Reference proteome;
KW RNA-binding; Toxin-antitoxin system.
FT CHAIN 1..104
FT /note="mRNA interferase HigB"
FT /id="PRO_0000169423"
FT HELIX 7..15
FT /evidence="ECO:0007829|PDB:5YCL"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:5YCL"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:5YCL"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:5YCL"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:5YCL"
FT TURN 63..66
FT /evidence="ECO:0007829|PDB:5YCL"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:5YCL"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:5YCL"
FT STRAND 79..87
FT /evidence="ECO:0007829|PDB:5YCL"
FT HELIX 88..96
FT /evidence="ECO:0007829|PDB:5YCL"
SQ SEQUENCE 104 AA; 12103 MW; F23FB5F433C52C22 CRC64;
MHLITQKALK DAAEKYPQHK TELVALGNTI AKGYFKKPES LKAVFPSLDN FKYLDKHYVF
NVGGNELRVV AMVFFESQKC YIREVMTHKE YDFFTAVHRT KGKK