CSY3_PSEAB
ID CSY3_PSEAB Reviewed; 342 AA.
AC Q02MM1;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=CRISPR-associated protein Csy3;
GN Name=csy3; Synonyms=csy1-3; OrderedLocusNames=PA14_33310;
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(2006).
RN [2]
RP FUNCTION IN INHIBITION OF BIOFILM FORMATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=UCBPP-PA14;
RX PubMed=21398535; DOI=10.1128/jb.01411-10;
RA Cady K.C., O'Toole G.A.;
RT "Non-identity-mediated CRISPR-bacteriophage interaction mediated via the
RT Csy and Cas3 proteins.";
RL J. Bacteriol. 193:3433-3445(2011).
RN [3]
RP NO ROLE IN PHAGE PROTECTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=UCBPP-PA14;
RX PubMed=21081758; DOI=10.1099/mic.0.045732-0;
RA Cady K.C., White A.S., Hammond J.H., Abendroth M.D., Karthikeyan R.S.,
RA Lalitha P., Zegans M.E., O'Toole G.A.;
RT "Prevalence, conservation and functional analysis of Yersinia and
RT Escherichia CRISPR regions in clinical Pseudomonas aeruginosa isolates.";
RL Microbiology 157:430-437(2011).
RN [4]
RP SUBUNIT, AND MASS SPECTROMETRY.
RC STRAIN=UCBPP-PA14;
RX PubMed=21536913; DOI=10.1073/pnas.1102716108;
RA Wiedenheft B., van Duijn E., Bultema J.B., Waghmare S.P., Zhou K.,
RA Barendregt A., Westphal W., Heck A.J., Boekema E.J., Dickman M.J.,
RA Doudna J.A.;
RT "RNA-guided complex from a bacterial immune system enhances target
RT recognition through seed sequence interactions.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:10092-10097(2011).
RN [5]
RP FUNCTION IN CRRNA FORMATION, AND SUBUNIT.
RC STRAIN=UCBPP-PA14;
RX PubMed=22522703; DOI=10.1038/emboj.2012.107;
RA Haurwitz R.E., Sternberg S.H., Doudna J.A.;
RT "Csy4 relies on an unusual catalytic dyad to position and cleave CRISPR
RT RNA.";
RL EMBO J. 31:2824-2832(2012).
CC -!- FUNCTION: CRISPR (clustered regularly interspaced short palindromic
CC repeat) is an adaptive immune system that provides protection against
CC mobile genetic elements (viruses, transposable elements and conjugative
CC plasmids). CRISPR clusters contain sequences complementary to
CC antecedent mobile elements and target invading nucleic acids. CRISPR
CC clusters are transcribed and processed into CRISPR RNA (crRNA). Cas3
CC and Cascade participate in CRISPR interference, the third stage of
CC CRISPR immunity (Potential). Involved in crRNA production or stability.
CC The Csy ribonucleoprotein complex binds target ssDNA with high affinity
CC but target dsDNA with much lower affinity.
CC {ECO:0000269|PubMed:21398535, ECO:0000269|PubMed:22522703,
CC ECO:0000305}.
CC -!- SUBUNIT: Part of the Csy ribonucleoprotein complex with a probable
CC stoichiometry of Csy1(1),Csy2(1),Csy3(6),Cas6/Csy4(1)-crRNA(1). A
CC Csy3(6),Cas6/Csy4(1)-crRNA(1) subcomplex is also formed.
CC {ECO:0000269|PubMed:21536913, ECO:0000269|PubMed:22522703}.
CC -!- INTERACTION:
CC Q02MM1; Q02MM2: cas6f; NbExp=12; IntAct=EBI-15924841, EBI-15924852;
CC -!- MASS SPECTROMETRY: Mass=37401.0; Mass_error=1.2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:21536913};
CC -!- DISRUPTION PHENOTYPE: Mutants lose phage DMS3 infection-dependent
CC inhibition of biofilm formation while there is normal biofilm formation
CC in the absence of phage infection. Decreased production of crRNA in the
CC presence or absence of phage. Disruption of the entire Y.pestis-subtype
CC CRISPR region disrupts crRNA production but does not alter phage
CC resistance (possibly OLNs PA14_33350 to PA14_33310, and the flanking
CC CRISPR loci), indicating this CRISPR is not involved in phage
CC resistance. {ECO:0000269|PubMed:21081758, ECO:0000269|PubMed:21398535}.
CC -!- MISCELLANEOUS: In this bacteria, Y.pestis-subtype CRISPRs do not confer
CC resistance to phage DMS3 or MP22, but instead are required for DMS3
CC infection-dependent inhibition of biofilm formation and possibly
CC motility.
CC -!- SIMILARITY: Belongs to the CRISPR-associated Csy3 family.
CC {ECO:0000305}.
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DR EMBL; CP000438; ABJ11604.1; -; Genomic_DNA.
DR RefSeq; WP_003139222.1; NZ_CP034244.1.
DR PDB; 5UZ9; EM; 3.40 A; C/D/E/F/G/H=2-342.
DR PDB; 5XLO; EM; 3.80 A; A/B/C/D/E/F=1-342.
DR PDB; 5XLP; EM; 4.20 A; C/D/E/F=1-342.
DR PDB; 6B44; EM; 2.90 A; C/D/E/F/G/H=1-342.
DR PDB; 6B45; EM; 3.50 A; C/D/E/F/G/H=1-342.
DR PDB; 6B46; EM; 3.10 A; C/D/E/F/G/H=1-342.
DR PDB; 6B47; EM; 3.20 A; C/D/E/F/G/H=1-342.
DR PDB; 6B48; EM; 3.60 A; C/D/E/F/G/H=1-342.
DR PDB; 6NE0; EM; 3.40 A; C/D/E/F/G/H=1-342.
DR PDBsum; 5UZ9; -.
DR PDBsum; 5XLO; -.
DR PDBsum; 5XLP; -.
DR PDBsum; 6B44; -.
DR PDBsum; 6B45; -.
DR PDBsum; 6B46; -.
DR PDBsum; 6B47; -.
DR PDBsum; 6B48; -.
DR PDBsum; 6NE0; -.
DR AlphaFoldDB; Q02MM1; -.
DR SMR; Q02MM1; -.
DR DIP; DIP-59680N; -.
DR IntAct; Q02MM1; 5.
DR PRIDE; Q02MM1; -.
DR EnsemblBacteria; ABJ11604; ABJ11604; PA14_33310.
DR KEGG; pau:PA14_33310; -.
DR HOGENOM; CLU_063672_0_0_6; -.
DR OMA; CNDQDYQ; -.
DR BioCyc; PAER208963:G1G74-2803-MON; -.
DR Proteomes; UP000000653; Chromosome.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR InterPro; IPR013399; CRISPR-assoc_prot_Csy3.
DR Pfam; PF09615; Cas_Csy3; 1.
DR TIGRFAMs; TIGR02566; cas_Csy3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense.
FT CHAIN 1..342
FT /note="CRISPR-associated protein Csy3"
FT /id="PRO_0000417878"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:6B46"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:6B46"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:6B46"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:6B47"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:6B46"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:6B46"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:6B44"
FT TURN 64..72
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:6B46"
FT STRAND 90..99
FT /evidence="ECO:0007829|PDB:6B46"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:6B46"
FT HELIX 112..127
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 132..143
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:6B47"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:6B46"
FT HELIX 192..203
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:6B44"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:6B46"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:6NE0"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 257..263
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:6B47"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:6NE0"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:6B47"
FT TURN 298..302
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 304..312
FT /evidence="ECO:0007829|PDB:6B44"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 323..332
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:6B46"
SQ SEQUENCE 342 AA; 37530 MW; D0C8687209C35F91 CRC64;
MSKPILSTAS VLAFERKLDP SDALMSAGAW AQRDASQEWP AVTVREKSVR GTISNRLKTK
DRDPAKLDAS IQSPNLQTVD VANLPSDADT LKVRFTLRVL GGAGTPSACN DAAYRDKLLQ
TVATYVNDQG FAELARRYAH NLANARFLWR NRVGAEAVEV RINHIRQGEV ARAWRFDALA
IGLRDFKADA ELDALAELIA SGLSGSGHVL LEVVAFARIG DGQEVFPSQE LILDKGDKKG
QKSKTLYSVR DAAAIHSQKI GNALRTIDTW YPDEDGLGPI AVEPYGSVTS QGKAYRQPKQ
KLDFYTLLDN WVLRDEAPAV EQQHYVIANL IRGGVFGEAE EK
