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MVFR_PSEAE
ID   MVFR_PSEAE              Reviewed;         332 AA.
AC   Q9I4X0;
DT   13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Multiple virulence factor regulator MvfR {ECO:0000303|PubMed:11724939};
DE   AltName: Full=Transcriptional regulator MvfR;
GN   Name=mvfR {ECO:0000303|PubMed:11724939}; OrderedLocusNames=PA1003;
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 [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   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11724939; DOI=10.1073/pnas.251465298;
RA   Cao H., Krishnan G., Goumnerov B., Tsongalis J., Tompkins R., Rahme L.G.;
RT   "A quorum sensing-associated virulence gene of Pseudomonas aeruginosa
RT   encodes a LysR-like transcription regulator with a unique self-regulatory
RT   mechanism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:14613-14618(2001).
RN   [3]
RP   FUNCTION, AND ACTIVITY REGULATION.
RX   PubMed=17083468; DOI=10.1111/j.1365-2958.2006.05462.x;
RA   Xiao G., Deziel E., He J., Lepine F., Lesic B., Castonguay M.H., Milot S.,
RA   Tampakaki A.P., Stachel S.E., Rahme L.G.;
RT   "MvfR, a key Pseudomonas aeruginosa pathogenicity LTTR-class regulatory
RT   protein, has dual ligands.";
RL   Mol. Microbiol. 62:1689-1699(2006).
RN   [4]
RP   FUNCTION.
RX   PubMed=27678057; DOI=10.1038/srep34083;
RA   Maura D., Hazan R., Kitao T., Ballok A.E., Rahme L.G.;
RT   "Evidence for direct control of virulence and defense gene circuits by the
RT   Pseudomonas aeruginosa quorum sensing regulator, MvfR.";
RL   Sci. Rep. 6:34083-34083(2016).
RN   [5] {ECO:0007744|PDB:6B8A}
RP   X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 94-295, AND SUBUNIT.
RX   PubMed=29339431; DOI=10.1128/mbio.02158-17;
RA   Kitao T., Lepine F., Babloudi S., Walte F., Steinbacher S., Maskos K.,
RA   Blaesse M., Negri M., Pucci M., Zahler B., Felici A., Rahme L.G.;
RT   "Molecular Insights into Function and Competitive Inhibition of Pseudomonas
RT   aeruginosa Multiple Virulence Factor Regulator.";
RL   MBio 9:0-0(2018).
CC   -!- FUNCTION: Transcription regulator that plays a critical role in
CC       virulence by positively regulating the expression of multiple quorum
CC       sensing (QS)-regulated virulence factors, genes involved in protein
CC       secretion, translation, response to oxidative stress and the phnAB
CC       operon (PubMed:11724939, PubMed:27678057, PubMed:17083468). At the
CC       stationary phase, negatively autoregulates its function through
CC       cleavage and translocation to the extracellular space
CC       (PubMed:11724939). {ECO:0000269|PubMed:11724939,
CC       ECO:0000269|PubMed:17083468, ECO:0000269|PubMed:27678057}.
CC   -!- ACTIVITY REGULATION: Both 3,4-dihydroxy-2-heptylquinoline (PQS) and its
CC       precursor 4-hydroxy-2-heptylquinoline (HHQ) function as ligands and
CC       promote MvfR DNA-binding activity leading to transcriptional
CC       activation. {ECO:0000269|PubMed:17083468}.
CC   -!- SUBUNIT: Forms homooligomers. {ECO:0000269|PubMed:29339431}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000269|PubMed:11724939}. Secreted {ECO:0000269|PubMed:11724939}.
CC       Note=At stationary phase, gets cleaved and subsequently released in the
CC       extracellular space where its transcriptional activity is inhibited.
CC       {ECO:0000269|PubMed:11724939}.
CC   -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC       {ECO:0000305}.
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DR   EMBL; AE004091; AAG04392.1; -; Genomic_DNA.
DR   PIR; D83519; D83519.
DR   RefSeq; NP_249694.1; NC_002516.2.
DR   RefSeq; WP_003108614.1; NZ_QZGE01000006.1.
DR   PDB; 6B8A; X-ray; 2.65 A; A/B=94-295.
DR   PDB; 6Q7U; X-ray; 3.14 A; A=91-319.
DR   PDB; 6Q7V; X-ray; 2.56 A; A/B=91-319.
DR   PDB; 6Q7W; X-ray; 2.82 A; A=91-319.
DR   PDB; 6YIZ; X-ray; 2.16 A; A/B=91-319.
DR   PDB; 7NBW; X-ray; 2.28 A; A=91-319.
DR   PDBsum; 6B8A; -.
DR   PDBsum; 6Q7U; -.
DR   PDBsum; 6Q7V; -.
DR   PDBsum; 6Q7W; -.
DR   PDBsum; 6YIZ; -.
DR   PDBsum; 7NBW; -.
DR   AlphaFoldDB; Q9I4X0; -.
DR   SMR; Q9I4X0; -.
DR   STRING; 287.DR97_945; -.
DR   PaxDb; Q9I4X0; -.
DR   DNASU; 879994; -.
DR   EnsemblBacteria; AAG04392; AAG04392; PA1003.
DR   GeneID; 879994; -.
DR   KEGG; pae:PA1003; -.
DR   PATRIC; fig|208964.12.peg.1035; -.
DR   PseudoCAP; PA1003; -.
DR   HOGENOM; CLU_060101_0_0_6; -.
DR   OMA; QEDYCMF; -.
DR   PhylomeDB; Q9I4X0; -.
DR   BioCyc; PAER208964:G1FZ6-1022-MON; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0051349; P:positive regulation of lyase activity; IMP:PseudoCAP.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   GO; GO:0034762; P:regulation of transmembrane transport; IMP:PseudoCAP.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR005119; LysR_subst-bd.
DR   InterPro; IPR000847; Tscrpt_reg_HTH_LysR.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00126; HTH_1; 1.
DR   Pfam; PF03466; LysR_substrate; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS50931; HTH_LYSR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell inner membrane; Cell membrane; DNA-binding; Membrane;
KW   Reference proteome; Secreted; Transcription; Transcription regulation;
KW   Virulence.
FT   CHAIN           1..332
FT                   /note="Multiple virulence factor regulator MvfR"
FT                   /id="PRO_0000448531"
FT   DOMAIN          4..61
FT                   /note="HTH lysR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT   DNA_BIND        21..40
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT   HELIX           92..94
FT                   /evidence="ECO:0007829|PDB:6YIZ"
FT   STRAND          95..100
FT                   /evidence="ECO:0007829|PDB:6YIZ"
FT   HELIX           105..118
FT                   /evidence="ECO:0007829|PDB:6YIZ"
FT   STRAND          122..127
FT                   /evidence="ECO:0007829|PDB:6YIZ"
FT   HELIX           129..131
FT                   /evidence="ECO:0007829|PDB:6YIZ"
FT   HELIX           132..137
FT                   /evidence="ECO:0007829|PDB:6YIZ"
FT   HELIX           139..141
FT                   /evidence="ECO:0007829|PDB:6YIZ"
FT   STRAND          145..149
FT                   /evidence="ECO:0007829|PDB:6YIZ"
FT   STRAND          156..172
FT                   /evidence="ECO:0007829|PDB:6YIZ"
FT   STRAND          174..176
FT                   /evidence="ECO:0007829|PDB:6B8A"
FT   HELIX           177..180
FT                   /evidence="ECO:0007829|PDB:6YIZ"
FT   STRAND          181..183
FT                   /evidence="ECO:0007829|PDB:6Q7V"
FT   HELIX           186..190
FT                   /evidence="ECO:0007829|PDB:6YIZ"
FT   STRAND          194..197
FT                   /evidence="ECO:0007829|PDB:6YIZ"
FT   STRAND          200..202
FT                   /evidence="ECO:0007829|PDB:6Q7V"
FT   TURN            206..208
FT                   /evidence="ECO:0007829|PDB:7NBW"
FT   STRAND          213..220
FT                   /evidence="ECO:0007829|PDB:6YIZ"
FT   HELIX           221..230
FT                   /evidence="ECO:0007829|PDB:6YIZ"
FT   STRAND          234..238
FT                   /evidence="ECO:0007829|PDB:6YIZ"
FT   HELIX           239..247
FT                   /evidence="ECO:0007829|PDB:6YIZ"
FT   STRAND          249..254
FT                   /evidence="ECO:0007829|PDB:6YIZ"
FT   TURN            256..258
FT                   /evidence="ECO:0007829|PDB:6YIZ"
FT   STRAND          263..272
FT                   /evidence="ECO:0007829|PDB:6YIZ"
FT   HELIX           273..277
FT                   /evidence="ECO:0007829|PDB:6YIZ"
FT   HELIX           279..297
FT                   /evidence="ECO:0007829|PDB:6YIZ"
FT   HELIX           298..300
FT                   /evidence="ECO:0007829|PDB:6YIZ"
SQ   SEQUENCE   332 AA;  37214 MW;  117430C3C1232D97 CRC64;
     MPIHNLNHVN MFLQVIASGS ISSAARILRK SHTAVSSAVS NLEIDLCVEL VRRDGYKVEP
     TEQALRLIPY MRSLLNYQQL IGDIAFNLNK GPRNLRVLLD TAIPPSFCDT VSSVLLDDFN
     MVSLIRTSPA DSLATIKQDN AEIDIAITID EELKISRFNQ CVLGYTKAFV VAHPQHPLCN
     ASLHSIASLA NYRQISLGSR SGQHSNLLRP VSDKVLFVEN FDDMLRLVEA GVGWGIAPHY
     FVEERLRNGT LAVLSELYEP GGIDTKVYCY YNTALESERS FLRFLESARQ RLRELGRQRF
     DDAPAWQPSI VETAQRRSGP KALAYRQRAA PE
 
 
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