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DBHA_SHIFL
ID   DBHA_SHIFL              Reviewed;          90 AA.
AC   P0ACF3; P02342;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=DNA-binding protein HU-alpha;
DE   AltName: Full=HU-2;
DE   AltName: Full=NS2;
GN   Name=hupA; OrderedLocusNames=SF4072, S3663;
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: Histone-like DNA-binding protein which is capable of wrapping
CC       DNA to stabilize it, and thus to prevent its denaturation under extreme
CC       environmental conditions. {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the bacterial histone-like protein family.
CC       {ECO:0000305}.
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DR   EMBL; AE005674; AAN45501.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP18700.1; -; Genomic_DNA.
DR   RefSeq; NP_709794.1; NC_004337.2.
DR   RefSeq; WP_001044513.1; NZ_WPGW01000040.1.
DR   AlphaFoldDB; P0ACF3; -.
DR   SMR; P0ACF3; -.
DR   STRING; 198214.SF4072; -.
DR   PRIDE; P0ACF3; -.
DR   EnsemblBacteria; AAN45501; AAN45501; SF4072.
DR   EnsemblBacteria; AAP18700; AAP18700; S3663.
DR   GeneID; 1027571; -.
DR   GeneID; 67415298; -.
DR   KEGG; sfl:SF4072; -.
DR   KEGG; sfx:S3663; -.
DR   PATRIC; fig|198214.7.peg.4796; -.
DR   HOGENOM; CLU_105066_3_1_6; -.
DR   OMA; ISQEKQC; -.
DR   OrthoDB; 1847472at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.520.10; -; 1.
DR   InterPro; IPR000119; Hist_DNA-bd.
DR   InterPro; IPR020816; Histone-like_DNA-bd_CS.
DR   InterPro; IPR010992; IHF-like_DNA-bd_dom_sf.
DR   PANTHER; PTHR33175; PTHR33175; 1.
DR   Pfam; PF00216; Bac_DNA_binding; 1.
DR   PRINTS; PR01727; DNABINDINGHU.
DR   SMART; SM00411; BHL; 1.
DR   SUPFAM; SSF47729; SSF47729; 1.
DR   PROSITE; PS00045; HISTONE_LIKE; 1.
PE   3: Inferred from homology;
KW   DNA condensation; DNA-binding; Reference proteome.
FT   CHAIN           1..90
FT                   /note="DNA-binding protein HU-alpha"
FT                   /id="PRO_0000104938"
SQ   SEQUENCE   90 AA;  9535 MW;  6B5B8536FDBD13DC CRC64;
     MNKTQLIDVI AEKAELSKTQ AKAALESTLA AITESLKEGD AVQLVGFGTF KVNHRAERTG
     RNPQTGKEIK IAAANVPAFV SGKALKDAVK
 
 
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