CSY1_PSEAB
ID CSY1_PSEAB Reviewed; 434 AA.
AC Q02ML9;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=CRISPR-associated protein Csy1;
GN Name=csy1; OrderedLocusNames=PA14_33330;
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 INTERACTION WITH CSY2, 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: Interacts directly with Csy2; 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 Q02ML9; Q02MM0: csy2; NbExp=6; IntAct=EBI-15924821, EBI-15924831;
CC -!- MASS SPECTROMETRY: Mass=49000.9; Mass_error=2.0; 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 Csy1 family.
CC {ECO:0000305}.
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DR EMBL; CP000438; ABJ11602.1; -; Genomic_DNA.
DR RefSeq; WP_003139224.1; NZ_CP034244.1.
DR PDB; 5UZ9; EM; 3.40 A; A=1-434.
DR PDB; 6B44; EM; 2.90 A; A=1-434.
DR PDB; 6B45; EM; 3.50 A; A=1-434.
DR PDB; 6B47; EM; 3.20 A; A=1-434.
DR PDB; 6B48; EM; 3.60 A; A=1-434.
DR PDB; 6NE0; EM; 3.40 A; A=1-434.
DR PDBsum; 5UZ9; -.
DR PDBsum; 6B44; -.
DR PDBsum; 6B45; -.
DR PDBsum; 6B47; -.
DR PDBsum; 6B48; -.
DR PDBsum; 6NE0; -.
DR AlphaFoldDB; Q02ML9; -.
DR SMR; Q02ML9; -.
DR DIP; DIP-59678N; -.
DR IntAct; Q02ML9; 5.
DR PRIDE; Q02ML9; -.
DR EnsemblBacteria; ABJ11602; ABJ11602; PA14_33330.
DR KEGG; pau:PA14_33330; -.
DR HOGENOM; CLU_038921_0_0_6; -.
DR OMA; CEKYWLD; -.
DR BioCyc; PAER208963:G1G74-2805-MON; -.
DR Proteomes; UP000000653; Chromosome.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR InterPro; IPR013397; CRISPR-assoc_prot_Csy1.
DR Pfam; PF09611; Cas_Csy1; 1.
DR TIGRFAMs; TIGR02564; cas_Csy1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense.
FT CHAIN 1..434
FT /note="CRISPR-associated protein Csy1"
FT /id="PRO_0000417876"
FT REGION 76..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 15..27
FT /evidence="ECO:0007829|PDB:6B44"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:5UZ9"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 40..47
FT /evidence="ECO:0007829|PDB:6B44"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 52..58
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:6NE0"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 117..122
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:6B44"
FT TURN 141..145
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 149..158
FT /evidence="ECO:0007829|PDB:6B44"
FT TURN 159..163
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:6NE0"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:6B47"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 196..207
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 214..223
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:5UZ9"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:6B44"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:6B47"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 298..306
FT /evidence="ECO:0007829|PDB:6B44"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:6B47"
FT TURN 313..316
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 322..340
FT /evidence="ECO:0007829|PDB:6B44"
FT TURN 341..343
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:6B47"
FT TURN 353..357
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 358..362
FT /evidence="ECO:0007829|PDB:6B44"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:6B47"
FT TURN 374..381
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 387..398
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 403..406
FT /evidence="ECO:0007829|PDB:6B44"
FT TURN 409..411
FT /evidence="ECO:0007829|PDB:6B45"
FT HELIX 412..428
FT /evidence="ECO:0007829|PDB:6B44"
FT HELIX 429..431
FT /evidence="ECO:0007829|PDB:5UZ9"
SQ SEQUENCE 434 AA; 49129 MW; A4793744A125607A CRC64;
MTSPLPTPTW QELRQFIESF IQERLQGKLD KLQPDEDDKR QTLLATHRRE AWLADAARRV
GQLQLVTHTL KPIHPDARGS NLHSLPQAPG QPGLAGSHEL GDRLVSDVVG NAAALDVFKF
LSLQYQGKNL LNWLTEDSAE ALQALSDNAE QAREWRQAFI GITTVKGAPA SHSLAKQLYF
PLPGSGYHLL APLFPTSLVH HVHALLREAR FGDAAKAARE ARSRQESWPH GFSEYPNLAI
QKFGGTKPQN ISQLNNERRG ENWLLPSLPP NWQRQNVNAP MRHSSVFEHD FGRTPEVSRL
TRTLQRFLAK TVHNNLAIRQ RRAQLVAQIC DEALQYAARL RELEPGWSAT PGCQLHDAEQ
LWLDPLRAQT DETFLQRRLR GDWPAEVGNR FANWLNRAVS SDSQILGSPE AAQWSQELSK
ELTMFKEILE DERD
