位置:首页 > 蛋白库 > BPHY_XANC8
BPHY_XANC8
ID   BPHY_XANC8              Reviewed;         634 AA.
AC   A0A0H2XCS3;
DT   07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Bacteriophytochrome {ECO:0000303|PubMed:27107635};
DE            Short=BphP;
DE   AltName: Full=XccBphP {ECO:0000303|PubMed:27107635};
GN   Name=bphP; OrderedLocusNames=XC_4241;
OS   Xanthomonas campestris pv. campestris (strain 8004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=314565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8004;
RX   PubMed=15899963; DOI=10.1101/gr.3378705;
RA   Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q.,
RA   Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., Zeng S.,
RA   Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B., Fang R.,
RA   Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.;
RT   "Comparative and functional genomic analyses of the pathogenicity of
RT   phytopathogen Xanthomonas campestris pv. campestris.";
RL   Genome Res. 15:757-767(2005).
RN   [2]
RP   FUNCTION, INDUCTION, OPERON, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP   CYS-13.
RC   STRAIN=8004;
RX   PubMed=27621284; DOI=10.15252/embr.201541691;
RA   Bonomi H.R., Toum L., Sycz G., Sieira R., Toscani A.M., Gudesblat G.E.,
RA   Leskow F.C., Goldbaum F.A., Vojnov A.A., Malamud F.;
RT   "Xanthomonas campestris attenuates virulence by sensing light through a
RT   bacteriophytochrome photoreceptor.";
RL   EMBO Rep. 17:1565-1577(2016).
RN   [3] {ECO:0007744|PDB:5AKP}
RP   X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 2-634 FORM PR IN COMPLEX WITH
RP   BILIVERDIN CHROMOPHORE, FUNCTION, SUBUNIT, AND DOMAIN.
RC   STRAIN=8004;
RX   PubMed=27107635; DOI=10.1016/j.jmb.2016.04.012;
RA   Otero L.H., Klinke S., Rinaldi J., Velazquez-Escobar F., Mroginski M.A.,
RA   Lopez M.F., Malamud F., Vojnov A.A., Hildebrandt P., Goldbaum F.A.,
RA   Bonomi H.R.;
RT   "Structure of the full-length bacteriophytochrome from the plant pathogen
RT   Xanthomonas campestris provides clues to its long-range signaling
RT   mechanism.";
RL   J. Mol. Biol. 428:3702-3720(2016).
CC   -!- FUNCTION: Photoreceptor which exists in two forms that are reversibly
CC       interconvertible by light: far-red light (733 nm) converts protein to
CC       the red-absorbing (Pr) form, while red light (630 nm) partly converts
CC       the protein to the far-red-absorbing (Pfr) form (PubMed:27107635).
CC       Regulates virulence of X.campestris pv. campestris on its host plants,
CC       perhaps by fine-tuning expression to ambient light levels and/or
CC       spatial cues (PubMed:27621284). The Pr form may sense light and
CC       partially inhibit virulence; in the dark (Pfr form) biofilm and
CC       xanathan production rise and bacteria are more virulent
CC       (PubMed:27621284). Strains overexpressing this protein have
CC       significantly decreased amounts of extracellular beta-1,4-
CC       endoglucanase, produce less xanthin and have decreased transcription of
CC       genes involved in virulence such as endoglucanases, type 2 secretion
CC       systems, xanthan production and flagellar-dependent motility
CC       (PubMed:27621284). {ECO:0000269|PubMed:27107635,
CC       ECO:0000269|PubMed:27621284, ECO:0000305|PubMed:27621284}.
CC   -!- SUBUNIT: Forms head-to-head homodimers (PubMed:27107635).
CC       {ECO:0000269|PubMed:27107635}.
CC   -!- INDUCTION: Expressed in dark and light (at protein level). Part of the
CC       bphO-bphP operon (PubMed:27621284). {ECO:0000269|PubMed:27621284}.
CC   -!- DOMAIN: Composed of 4 domains; in the N-terminus the PAS2-GAF-PHY
CC       domains form the photosensor while the C-terminal PAS9 domain is the
CC       output module. Long linker helices serve as connectors within the GAF-
CC       PHY and PHY-PAS9 domain pairs, forming a helical spine where the dimer
CC       interface is assembled. Thus both the photosensor and PAS9 domains are
CC       required for dimerization. Within the PHY domain is the mobile tongue
CC       domain (residues 452-480) that probably serves as a gatekeeper to the
CC       chromophore-binding pocket, in the Pr form it is a beta-sheet, in a
CC       R.palustris Pfr crystal it is an alpha helix (AC B3Q7C0). In the dark
CC       (Pfr) state the protein is compact and protease resistant, far-red
CC       light treated protein (Pr) is quickly degraded to its domains, with
CC       important cuts occurring in the hinge region (just before the PAS9
CC       output domain at about residue 512) and in the tongue domain (about
CC       residue 469). {ECO:0000305|PubMed:27107635}.
CC   -!- PTM: Contains one covalently linked biliverdin IX-alpha chromophore;
CC       present in the crystal structure as a mixture of Pr and Meta-R
CC       configurations. {ECO:0000269|PubMed:27107635}.
CC   -!- DISRUPTION PHENOTYPE: No growth phenotype in liquid culture, slightly
CC       better growth on plates, strain loses slight sensitivity to white
CC       light. In planta is more virulent, with increased growth in host
CC       (A.thaliana) leaves, mutant opens leaf stomata better than wild-type,
CC       has decreased leaf callose deposits, produces more xanthan than wild-
CC       type and is insensitive to white light, has considerably increased
CC       sliding and slightly increased swimming mobility, generates mature
CC       biofilm in the light and dark. {ECO:0000269|PubMed:27621284}.
CC   -!- MISCELLANEOUS: X.campestris pv. campestris colonizes plant leaves and
CC       is responsible for black rot in cruciferous plants (Brassicaceae). In
CC       the cruciferous model host organism A.thaliana, morning and midday
CC       infections result in more hypersensitive responses than evening or
CC       night infections, suggesting light plays a role in virulence.
CC       {ECO:0000305|PubMed:27621284}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000050; AAY51279.1; -; Genomic_DNA.
DR   RefSeq; WP_011270102.1; NC_007086.1.
DR   PDB; 5AKP; X-ray; 3.25 A; A/B=2-634.
DR   PDB; 5UYR; X-ray; 3.45 A; A/B=2-634.
DR   PDB; 6NDO; X-ray; 3.58 A; A/B=2-634.
DR   PDB; 6NDP; X-ray; 3.89 A; A/B=2-634.
DR   PDB; 6PL0; X-ray; 2.96 A; A/B=2-634.
DR   PDB; 7L59; X-ray; 2.68 A; A=2-634.
DR   PDB; 7L5A; X-ray; 2.95 A; A=2-511.
DR   PDBsum; 5AKP; -.
DR   PDBsum; 5UYR; -.
DR   PDBsum; 6NDO; -.
DR   PDBsum; 6NDP; -.
DR   PDBsum; 6PL0; -.
DR   PDBsum; 7L59; -.
DR   PDBsum; 7L5A; -.
DR   AlphaFoldDB; A0A0H2XCS3; -.
DR   SMR; A0A0H2XCS3; -.
DR   EnsemblBacteria; AAY51279; AAY51279; XC_4241.
DR   KEGG; xcb:XC_4241; -.
DR   HOGENOM; CLU_000445_50_5_6; -.
DR   OMA; YMRNIGM; -.
DR   OrthoDB; 1635706at2; -.
DR   PHI-base; PHI:7645; -.
DR   Proteomes; UP000000420; Chromosome.
DR   GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 3.30.450.270; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013654; PAS_2.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR016132; Phyto_chromo_attachment.
DR   InterPro; IPR001294; Phytochrome.
DR   InterPro; IPR013515; Phytochrome_cen-reg.
DR   InterPro; IPR043150; Phytochrome_PHY.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF08446; PAS_2; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF00360; PHY; 1.
DR   PRINTS; PR01033; PHYTOCHROME.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF55785; SSF55785; 2.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50046; PHYTOCHROME_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chromophore; Photoreceptor protein; Receptor;
KW   Sensory transduction; Virulence.
FT   CHAIN           1..634
FT                   /note="Bacteriophytochrome"
FT                   /id="PRO_0000437191"
FT   DOMAIN          13..118
FT                   /note="PAS 1"
FT                   /evidence="ECO:0000305|PubMed:27107635"
FT   DOMAIN          151..305
FT                   /note="GAF"
FT                   /evidence="ECO:0000305|PubMed:27107635"
FT   DOMAIN          515..590
FT                   /note="PAS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   REGION          13..514
FT                   /note="Photosensory core domain"
FT                   /evidence="ECO:0000305|PubMed:27107635"
FT   REGION          325..508
FT                   /note="Phytochrome-specific (PHY)"
FT                   /evidence="ECO:0000305|PubMed:27107635"
FT   REGION          452..480
FT                   /note="Tongue domain"
FT                   /evidence="ECO:0000305|PubMed:27107635"
FT   REGION          515..634
FT                   /note="PAS9, output module, not required to bind biliverdin
FT                   IX-alpha, required for dimerization"
FT                   /evidence="ECO:0000305|PubMed:27107635"
FT   BINDING         13
FT                   /ligand="biliverdin IXalpha"
FT                   /ligand_id="ChEBI:CHEBI:57991"
FT                   /note="covalent, via 1 link"
FT                   /evidence="ECO:0000269|PubMed:27107635"
FT   MUTAGEN         13
FT                   /note="C->S: Loss of photo-inducible Pr-Pfr conversion;
FT                   protein still binds pigment. No difference in growth in
FT                   host, increased callose deposits, increased xanthan
FT                   production, increased sliding and swimming mobility."
FT                   /evidence="ECO:0000269|PubMed:27621284"
FT   HELIX           12..15
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   STRAND          22..24
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   STRAND          28..33
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   TURN            35..37
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   STRAND          39..44
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   HELIX           47..51
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   HELIX           55..58
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   HELIX           63..66
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   STRAND          78..80
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   STRAND          82..90
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   STRAND          94..96
FT                   /evidence="ECO:0007829|PDB:6PL0"
FT   STRAND          102..108
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   STRAND          113..121
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   HELIX           129..139
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   HELIX           145..159
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   STRAND          163..170
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   STRAND          176..183
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   STRAND          185..187
FT                   /evidence="ECO:0007829|PDB:5AKP"
FT   STRAND          193..195
FT                   /evidence="ECO:0007829|PDB:5AKP"
FT   HELIX           197..199
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   HELIX           202..211
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   STRAND          212..217
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   STRAND          224..230
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   TURN            232..234
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   HELIX           250..259
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   STRAND          263..271
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   STRAND          274..285
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   HELIX           291..332
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   TURN            333..336
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   STRAND          337..339
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   HELIX           343..347
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   HELIX           349..354
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   TURN            355..357
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   STRAND          359..365
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   STRAND          368..371
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   HELIX           378..390
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   HELIX           391..393
FT                   /evidence="ECO:0007829|PDB:6PL0"
FT   HELIX           394..399
FT                   /evidence="ECO:0007829|PDB:6PL0"
FT   STRAND          402..408
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   HELIX           409..412
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   HELIX           414..419
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   HELIX           420..423
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   STRAND          424..431
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   STRAND          432..434
FT                   /evidence="ECO:0007829|PDB:6PL0"
FT   STRAND          435..443
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   HELIX           446..449
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   STRAND          452..454
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   TURN            456..460
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   HELIX           471..481
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   TURN            482..484
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   HELIX           491..510
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   HELIX           518..524
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   STRAND          531..534
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   STRAND          538..540
FT                   /evidence="ECO:0007829|PDB:6PL0"
FT   STRAND          543..547
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   HELIX           549..555
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   HELIX           559..562
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   TURN            568..571
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   STRAND          578..580
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   HELIX           581..587
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   TURN            588..590
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   STRAND          596..598
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   STRAND          608..610
FT                   /evidence="ECO:0007829|PDB:7L59"
FT   STRAND          619..622
FT                   /evidence="ECO:0007829|PDB:5AKP"
FT   STRAND          625..629
FT                   /evidence="ECO:0007829|PDB:7L59"
SQ   SEQUENCE   634 AA;  70355 MW;  0E6FECCC240F6F45 CRC64;
     MSTATNPLDL DVCAREPIHI PGLIQPYGVL LVIDPADGRI VQASTTAADL LGVPMAALLG
     MPYTQVLTLP EAQPFAVDDQ PQHLMHAEVR FPQRATPPAS AWVAAWHLYP QQWLVEMEPR
     DARLLDVTLR EAMPLLRSVE RDPGIAEAAV RVAKGLRSLI GFDRVMIYRF DEEWNGDIIA
     EARKPELEAY LGLHYPASDI PAQARALYLR NRVRQIADVG YQPSPIQPTV HPQLGTPVDL
     SDVSLRSVSP VHLEYLANMG VTATLVASIV VNDALWGLIS CHHYSPHFTN HAMRDVTDAV
     ARTLAGRIGA LQAVARARLE SVLLTVREKL ITDFNDAEHM TVELLDDMAP DLMDVVDADG
     VAIFHGNDIS RHGTTPDVAA LRRIRDHIES EHHEALREDA VGALHVDAIG EVFPELADLA
     PLAAGFIFVP LMPQSRSALL WTRREQIQQI KWAGNPQLAK LEDIPNSRLS PRKSFDLWQQ
     TVRGRARRWS PLHLESARSL RVLIELMERK RFQQDFTLLE ASLSRLRDGV AIIERGTANA
     AHRLLFVNTA FADVCGSDVA ELIGRELQTL YASDAPRANV ELLQDALRNG RAAYVTLPLQ
     VSDGAPVYRQ FHLEPLPSPS GVTAHWLLQL RDPE
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024