CSY2_PSEAB
ID CSY2_PSEAB Reviewed; 327 AA.
AC Q02MM0;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=CRISPR-associated protein Csy2;
GN Name=csy2; OrderedLocusNames=PA14_33320;
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 CRRNA FORMATION, FUNCTION IN INHIBITION OF BIOFILM FORMATION,
RP 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 INTERACTION WITH CSY1, 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). Absolutely required for crRNA production
CC or stability. The Csy ribonucleoprotein complex binds target ssDNA with
CC high affinity but target dsDNA with much lower affinity.
CC {ECO:0000269|PubMed:21398535, ECO:0000269|PubMed:22522703,
CC ECO:0000305}.
CC -!- SUBUNIT: Interacts directly with Csy1; part of the Csy
CC ribonucleoprotein complex with a probable stoichiometry of
CC Csy1(1),Csy2(1),Csy3(6),Cas6/Csy4(1)-crRNA(1). A Csy3(6),Cas6/Csy4(1)-
CC crRNA(1) subcomplex is also formed. {ECO:0000269|PubMed:21536913,
CC ECO:0000269|PubMed:22522703}.
CC -!- INTERACTION:
CC Q02MM0; Q02ML9: csy1; NbExp=6; IntAct=EBI-15924831, EBI-15924821;
CC -!- MASS SPECTROMETRY: Mass=36071.7; Mass_error=1.7; 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. Loss of 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 Csy2 family.
CC {ECO:0000305}.
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DR EMBL; CP000438; ABJ11603.1; -; Genomic_DNA.
DR RefSeq; WP_003116910.1; NZ_CP034244.1.
DR PDB; 5UZ9; EM; 3.40 A; B=1-327.
DR PDB; 6B44; EM; 2.90 A; B=1-327.
DR PDB; 6B45; EM; 3.50 A; B=1-327.
DR PDB; 6B47; EM; 3.20 A; B=1-327.
DR PDB; 6B48; EM; 3.60 A; B=1-327.
DR PDB; 6NE0; EM; 3.40 A; B=1-327.
DR PDBsum; 5UZ9; -.
DR PDBsum; 6B44; -.
DR PDBsum; 6B45; -.
DR PDBsum; 6B47; -.
DR PDBsum; 6B48; -.
DR PDBsum; 6NE0; -.
DR AlphaFoldDB; Q02MM0; -.
DR SMR; Q02MM0; -.
DR DIP; DIP-59679N; -.
DR IntAct; Q02MM0; 4.
DR PRIDE; Q02MM0; -.
DR EnsemblBacteria; ABJ11603; ABJ11603; PA14_33320.
DR KEGG; pau:PA14_33320; -.
DR HOGENOM; CLU_073578_0_0_6; -.
DR OMA; MWALERK; -.
DR BioCyc; PAER208963:G1G74-2804-MON; -.
DR Proteomes; UP000000653; Chromosome.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR InterPro; IPR013398; CRISPR-assoc_prot_Csy2.
DR Pfam; PF09614; Cas_Csy2; 1.
DR TIGRFAMs; TIGR02565; cas_Csy2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense.
FT CHAIN 1..327
FT /note="CRISPR-associated protein Csy2"
FT /id="PRO_0000417877"
FT STRAND 7..21
FT /evidence="ECO:0007829|PDB:6B44"
FT TURN 24..27
FT /evidence="ECO:0007829|PDB:6B47"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 34..45
FT /evidence="ECO:0007829|PDB:6B44"
FT TURN 46..53
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:6B47"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:6B47"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:5UZ9"
FT STRAND 102..113
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 123..134
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:6B45"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 169..176
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:6NE0"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 191..195
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:6B44"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:6B44"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:6B45"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 252..259
FT /evidence="ECO:0007829|PDB:6B44"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 277..284
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 303..308
FT /evidence="ECO:0007829|PDB:6B47"
FT TURN 309..312
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:6B47"
SQ SEQUENCE 327 AA; 36201 MW; E2FAAD7F314BA9E1 CRC64;
MSVTDPEALL LLPRLSIQNA NAISSPLTWG FPSPGAFTGF VHALQRRVGI SLDIELDGVG
IVCHRFEAQI SQPAGKRTKV FNLTRNPLNR DGSTAAIVEE GRAHLEVSLL LGVHGDGLDD
HPAQEIARQV QEQAGAMRLA GGSILPWCNE RFPAPNAELL MLGGSDEQRR KNQRRLTRRL
LPGFALVSRE ALLQQHLETL RTTLPEATTL DALLDLCRIN FEPPATSSEE EASPPDAAWQ
VRDKPGWLVP IPAGYNALSP LYLPGEVRNA RDRETPLRFV ENLFGLGEWL SPHRVAALSD
LLWYHHAEPD KGLYRWSTPR FVEHAIA
