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Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7

DescriptionRecName: Full=DNA gyrase inhibitor {ECO:0000255|HAMAP-Rule:MF_01896};
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MyHits synonymsSBMC_SHIB3 , B2TYH1 , C85BCD23F28C274E
match map segment
ipfam:GyrI-like ihamap:DNA_gyrase_inhibitor ismart:AraC_E_bind  
ID   SBMC_SHIB3              Reviewed;         157 AA.
AC   B2TYH1;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   02-NOV-2016, entry version 44.
DE   RecName: Full=DNA gyrase inhibitor {ECO:0000255|HAMAP-Rule:MF_01896};
GN   Name=sbmC {ECO:0000255|HAMAP-Rule:MF_01896}; Synonyms=gyrI;
GN   OrderedLocusNames=SbBS512_E1226;
OS   Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=344609;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 3083-94 / BS512;
RA   Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA   Jiang L., Ravel J., Sebastian Y.;
RT   "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Inhibits the supercoiling activity of DNA gyrase. Acts
CC       by inhibiting DNA gyrase at an early step, prior to (or at the
CC       step of) binding of DNA by the gyrase. It protects cells against
CC       toxins that target DNA gyrase, by inhibiting activity of these
CC       toxins and reducing the formation of lethal double-strand breaks
CC       in the cell. {ECO:0000255|HAMAP-Rule:MF_01896}.
CC   -!- SUBUNIT: Interacts with DNA gyrase. {ECO:0000255|HAMAP-
CC       Rule:MF_01896}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01896}.
CC   -!- SIMILARITY: Belongs to the DNA gyrase inhibitor family.
CC       {ECO:0000255|HAMAP-Rule:MF_01896}.
DR   EMBL; CP001063; ACD07849.1; -; Genomic_DNA.
DR   RefSeq; WP_001105415.1; NC_010658.1.
DR   ProteinModelPortal; B2TYH1; -.
DR   SMR; B2TYH1; -.
DR   EnsemblBacteria; ACD07849; ACD07849; SbBS512_E1226.
DR   KEGG; sbc:SbBS512_E1226; -.
DR   PATRIC; 18669119; VBIShiBoy129590_1348.
DR   HOGENOM; HOG000121896; -.
DR   KO; K07470; -.
DR   OMA; TPWYQFF; -.
DR   Proteomes; UP000001030; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008657; F:DNA topoisomerase (ATP-hydrolyzing) inhibitor activity; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.20.80.10; -; 1.
DR   HAMAP; MF_01896; DNA_gyrase_inhibitor; 1.
DR   InterPro; IPR010499; AraC_E-bd.
DR   InterPro; IPR024911; DNA_gyrase_inhibitor_GyrI.
DR   InterPro; IPR029442; GyrI-like.
DR   InterPro; IPR011256; Reg_factor_effector_dom.
DR   Pfam; PF06445; GyrI-like; 1.
DR   SMART; SM00871; AraC_E_bind; 1.
DR   SUPFAM; SSF55136; SSF55136; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Stress response.
FT   CHAIN         1    157       DNA gyrase inhibitor.
FT                                /FTId=PRO_0000409707.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT         1    152       ipfam:GyrI-like [T]
FT   MYHIT         1    155       ihamap:DNA_gyrase_inhibitor [T]
FT   MYHIT         1    153       ismart:AraC_E_bind [T]
SQ   SEQUENCE   157 AA;  18081 MW;  C85BCD23F28C274E CRC64;
     MNYEIKQEEK RTVAGFHLVG PWEQTVKKGF EQLMMWVDSK NIVPKEWVAV YYDNPDETPA
     EKLRCDTVVT VPGYFTLPEN SEGVILTEIT GGQYAVAVAR VVGDDFAKPW YQFFNSLLQD
     SAYEMLPKPC FEVYLNNGAE DGYWDIEMYV AVQPKHH
//