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ALGB_PSEAE
ID   ALGB_PSEAE              Reviewed;         449 AA.
AC   P23747;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 166.
DE   RecName: Full=Alginate biosynthesis transcriptional regulatory protein AlgB;
GN   Name=algB; OrderedLocusNames=PA5483;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FRD1;
RX   PubMed=1899859; DOI=10.1128/jb.173.4.1406-1413.1991;
RA   Wozniak D.J., Ohman D.E.;
RT   "Pseudomonas aeruginosa AlgB, a two-component response regulator of the
RT   NtrC family, is required for algD transcription.";
RL   J. Bacteriol. 173:1406-1413(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1738315; DOI=10.1111/j.1365-2958.1992.tb00837.x;
RA   Goldberg J.B., Dahnke T.;
RT   "Pseudomonas aeruginosa AlgB, which modulates the expression of alginate,
RT   is a member of the NtrC subclass of prokaryotic regulators.";
RL   Mol. Microbiol. 6:59-66(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
RN   [4]
RP   CHARACTERIZATION, PHOSPHORYLATION AT ASP-59, AND MUTAGENESIS OF ASP-59.
RC   STRAIN=FRD1;
RX   PubMed=9473053; DOI=10.1128/jb.180.4.956-968.1998;
RA   Ma S., Selvaraj U., Ohman D.E., Quarless R., Hassett D.J., Wozniak D.J.;
RT   "Phosphorylation-independent activity of the response regulators AlgB and
RT   AlgR in promoting alginate biosynthesis in mucoid Pseudomonas aeruginosa.";
RL   J. Bacteriol. 180:956-968(1998).
CC   -!- FUNCTION: Member of the two-component regulatory system AlgB/KinB
CC       involved in regulation of alginate biosynthesis genes. Positive
CC       regulator of the alginate biosynthetic gene AlgD.
CC   -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis [regulation].
CC   -!- PTM: Phosphorylated by KinB. {ECO:0000269|PubMed:9473053}.
CC   -!- MISCELLANEOUS: In vivo phosphorylation of AlgB is not required for its
CC       role in alginate production. The mechanism by which it activates AlgD
CC       appears not to be mediated by conventional phosphorylation-dependent
CC       signal transduction.
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DR   EMBL; M62902; AAA25700.1; -; Genomic_DNA.
DR   EMBL; M82823; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AE004091; AAG08868.1; -; Genomic_DNA.
DR   PIR; A38449; A38449.
DR   RefSeq; NP_254170.1; NC_002516.2.
DR   RefSeq; WP_003102840.1; NZ_QZGE01000012.1.
DR   AlphaFoldDB; P23747; -.
DR   SMR; P23747; -.
DR   STRING; 287.DR97_2861; -.
DR   PaxDb; P23747; -.
DR   PRIDE; P23747; -.
DR   EnsemblBacteria; AAG08868; AAG08868; PA5483.
DR   GeneID; 877696; -.
DR   KEGG; pae:PA5483; -.
DR   PATRIC; fig|208964.12.peg.5748; -.
DR   PseudoCAP; PA5483; -.
DR   HOGENOM; CLU_000445_0_6_6; -.
DR   InParanoid; P23747; -.
DR   OMA; DMSPAIQ; -.
DR   PhylomeDB; P23747; -.
DR   BioCyc; PAER208964:G1FZ6-5610-MON; -.
DR   UniPathway; UPA00286; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0042121; P:alginic acid biosynthetic process; IMP:PseudoCAP.
DR   GO; GO:1900232; P:negative regulation of single-species biofilm formation on inanimate substrate; IMP:PseudoCAP.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   GO; GO:2000147; P:positive regulation of cell motility; IMP:PseudoCAP.
DR   GO; GO:0045862; P:positive regulation of proteolysis; IMP:PseudoCAP.
DR   GO; GO:1900378; P:positive regulation of secondary metabolite biosynthetic process; IMP:PseudoCAP.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:PseudoCAP.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR002197; HTH_Fis.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR002078; Sigma_54_int.
DR   InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR   InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR   InterPro; IPR025944; Sigma_54_int_dom_CS.
DR   Pfam; PF02954; HTH_8; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF00158; Sigma54_activat; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
DR   PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
DR   PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR   PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR   PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE   1: Evidence at protein level;
KW   Activator; Alginate biosynthesis; ATP-binding; DNA-binding;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Two-component regulatory system.
FT   CHAIN           1..449
FT                   /note="Alginate biosynthesis transcriptional regulatory
FT                   protein AlgB"
FT                   /id="PRO_0000081004"
FT   DOMAIN          10..124
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DOMAIN          147..376
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   DNA_BIND        426..445
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250"
FT   BINDING         175..182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   BINDING         238..247
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   MOD_RES         59
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169,
FT                   ECO:0000269|PubMed:9473053"
FT   MUTAGEN         59
FT                   /note="D->N: No phosphorylation; no effect on alginate
FT                   production."
FT                   /evidence="ECO:0000269|PubMed:9473053"
SQ   SEQUENCE   449 AA;  49323 MW;  E6452B88457CBC17 CRC64;
     METTSEKQGR ILLVDDESAI LRTFRYCLED EGYSVATASS APQAEALLQR QVFDLCFLDL
     RLGEDNGLDV LAQMRVQAPW MRVVIVTAHS AVDTAVDAMQ AGAVDYLVKP CSPDQLRLAA
     AKQLEVRQLT ARLEALEDEV RRQGDGLESH SPAMAAVLET ARQVAATDAN ILILGESGSG
     KGELARAIHT WSKRAKKPQV TINCPSLTAE LMESELFGHS RGAFTGATES TLGRVSQADG
     GTLFLDEIGD FPLTLQPKLL RFIQDKEYER VGDPVTRRAD VRILAATNRD LGAMVAQGQF
     REDLLYRLNV IVLNLPPLRE RAEDILGLAE RFLARFVKDY GRPARGFSEA AREAMRQYPW
     PGNVRELRNV IERASIICNQ ELVDVDHLGF SAAQSASSAP RIGESLSLED LEKAHITAVM
     ASSATLDQAA KTLGIDASTL YRKRKQYGL
 
 
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