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DASA_STRCO
ID   DASA_STRCO              Reviewed;         425 AA.
AC   Q9K491;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Diacetylchitobiose binding protein DasA {ECO:0000305};
DE   Flags: Precursor;
GN   Name=dasA {ECO:0000303|PubMed:17351098};
GN   OrderedLocusNames=SCO5232 {ECO:0000312|EMBL:CAB94617.1};
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
RN   [2]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=17351098; DOI=10.1128/aem.02612-06;
RA   Saito A., Shinya T., Miyamoto K., Yokoyama T., Kaku H., Minami E.,
RA   Shibuya N., Tsujibo H., Nagata Y., Ando A., Fujii T., Miyashita K.;
RT   "The dasABC gene cluster, adjacent to dasR, encodes a novel ABC transporter
RT   for the uptake of N,N'-diacetylchitobiose in Streptomyces coelicolor
RT   A3(2).";
RL   Appl. Environ. Microbiol. 73:3000-3008(2007).
RN   [3]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=18227241; DOI=10.1099/mic.0.2007/011940-0;
RA   Colson S., van Wezel G.P., Craig M., Noens E.E., Nothaft H., Mommaas A.M.,
RA   Titgemeyer F., Joris B., Rigali S.;
RT   "The chitobiose-binding protein, DasA, acts as a link between chitin
RT   utilization and morphogenesis in Streptomyces coelicolor.";
RL   Microbiology 154:373-382(2008).
RN   [4]
RP   SUBUNIT.
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=18957589; DOI=10.1099/mic.0.2008/019612-0;
RA   Saito A., Fujii T., Shinya T., Shibuya N., Ando A., Miyashita K.;
RT   "The msiK gene, encoding the ATP-hydrolysing component of N,N'-
RT   diacetylchitobiose ABC transporters, is essential for induction of
RT   chitinase production in Streptomyces coelicolor A3(2).";
RL   Microbiology 154:3358-3365(2008).
CC   -!- FUNCTION: Part of the ABC transporter complex DasABC-MsiK involved in
CC       N,N'-diacetylchitobiose ((GlcNAc)2) uptake. Binds specifically to
CC       (GlcNAc)2. Can also bind to GlcNAc, (GlcNAc)3, (GlcNAc)4 and (GlcNAc)5,
CC       but it exhibits the highest affinity for (GlcNAc)2 (PubMed:17351098).
CC       Involved in the control of morphological differentiation
CC       (PubMed:18227241). {ECO:0000269|PubMed:17351098,
CC       ECO:0000269|PubMed:18227241}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (MsiK),
CC       two transmembrane proteins (DasB and DasC) and a solute-binding protein
CC       (DasA). {ECO:0000305|PubMed:18957589}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC   -!- INDUCTION: Strongly induced by (GlcNAc)2, (GlcNAc)3 and colloidal
CC       chitin (PubMed:17351098, PubMed:18227241). Repressed by DasR
CC       (PubMed:18227241). {ECO:0000269|PubMed:17351098,
CC       ECO:0000269|PubMed:18227241}.
CC   -!- DISRUPTION PHENOTYPE: Disruption of the gene decreases (GlcNAc)2
CC       uptake. Mutant shows higher chitinase activity (PubMed:17351098). Null
CC       mutant shows medium-dependent development, only failing to produce
CC       aerial hyphae and spores on glucose-containig media. Under conditions
CC       that allow sporulation, highly aberrant spores with many prematurely
CC       produced germ tubes are observed (PubMed:18227241).
CC       {ECO:0000269|PubMed:17351098, ECO:0000269|PubMed:18227241}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AL939123; CAB94617.1; -; Genomic_DNA.
DR   RefSeq; NP_629379.1; NC_003888.3.
DR   RefSeq; WP_003973739.1; NZ_VNID01000008.1.
DR   AlphaFoldDB; Q9K491; -.
DR   SMR; Q9K491; -.
DR   STRING; 100226.SCO5232; -.
DR   GeneID; 1100673; -.
DR   KEGG; sco:SCO5232; -.
DR   PATRIC; fig|100226.15.peg.5315; -.
DR   eggNOG; COG2182; Bacteria.
DR   HOGENOM; CLU_031285_10_1_11; -.
DR   InParanoid; Q9K491; -.
DR   OMA; FIGMGWE; -.
DR   PhylomeDB; Q9K491; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR   InterPro; IPR006059; SBP.
DR   Pfam; PF01547; SBP_bac_1; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW   Signal; Sugar transport; Transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           21..425
FT                   /note="Diacetylchitobiose binding protein DasA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT                   /id="PRO_5004327847"
FT   LIPID           21
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           21
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   425 AA;  45292 MW;  302BED2FB23A3D27 CRC64;
     MKRKLIAAIG IAGMMVSIAA CGGDSDDDGK KAGADGYAGE TLTVWVMDGS SPDDWQADLA
     KDFEAKTKAK VKFEIQKWNG IQQKLTTALS EENPPDVFEI GNTQTPAYAK TGGLADLSDL
     KGEIGTDWSE SLNKSAVFDG KQYAAPWFVV NRVVVYNKKI WADAGIKELP KTRDEFYNDL
     KTIGEKTDAE PIYLPGQNWY HFVGLVIGEG GELVKKDGDK YVSNLADPKV AAATETYKKF
     QALSKAPKDK DEATPQQGEI FAKGKTGSFI GMGWEGATAI ATNPAIEKDL GYFTIPGPTA
     DKPEGVFLGG SNLAVAAGSK KQDLAKEFLK LALSDKYEGG LAKANGVIPN KEALQSNLKG
     NAAAEAAAPA AGTGDTTPLI PEWAAVENDP NPIKTYLTAV MKGKSPADAA KQVEGEFNKR
     LAQQQ
 
 
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