CAS3_PSEAB
ID CAS3_PSEAB Reviewed; 1076 AA.
AC Q02ML8;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=CRISPR-associated nuclease/helicase Cas3 subtype I-F/YPEST;
DE EC=3.1.-.-;
DE EC=3.6.4.-;
GN Name=cas3; OrderedLocusNames=PA14_33340;
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 POSSIBLE FUNCTION.
RX PubMed=18952788; DOI=10.1128/jb.00797-08;
RA Zegans M.E., Wagner J.C., Cady K.C., Murphy D.M., Hammond J.H.,
RA O'Toole G.A.;
RT "Interaction between bacteriophage DMS3 and host CRISPR region inhibits
RT group behaviors of Pseudomonas aeruginosa.";
RL J. Bacteriol. 191:210-219(2009).
RN [3]
RP FUNCTION IN INHIBITION OF BIOFILM FORMATION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF ASP-124 AND ASP-576.
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 [4]
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).
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 plus Cascade participate in CRISPR interference, the third stage of
CC CRISPR immunity (Potential). {ECO:0000305}.
CC -!- FUNCTION: In this bacteria Y.pestis-subtype CRISPRs do not confer
CC resistance to phage DSM3 or MP22, but instead are required for DMS3-
CC dependent inhibition of biofilm formation and possibly motility.
CC {ECO:0000269|PubMed:21398535}.
CC -!- SUBUNIT: Interacts with Cas1. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Infection with phage DSM3 inhibits biofilm
CC formation; disrupting this gene restores biofilm formation upon
CC infection with DMS3 infection. Normal biofilm formation in the absence
CC of phage infection. Decreased production of crRNA in the presence or
CC absence of phage. Disruption of the entire Y.pestis-subtype CRISPR
CC region disrupts crRNA production but does not alter phage resistance
CC (possibly OLNs PA14_33350 to PA14_33310, plus the flanking CRISPR
CC loci), indicating this CRISPR is not involved in phage resistance.
CC {ECO:0000269|PubMed:21081758, ECO:0000269|PubMed:21398535}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CRISPR-associated
CC nuclease Cas3-HD family. {ECO:0000305}.
CC -!- SIMILARITY: In the central section; belongs to the CRISPR-associated
CC helicase Cas3 family. {ECO:0000305}.
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DR EMBL; CP000438; ABJ11601.1; -; Genomic_DNA.
DR RefSeq; WP_003139227.1; NZ_CP034244.1.
DR PDB; 5B7I; X-ray; 2.60 A; A=1-1076.
DR PDB; 5GQH; EM; 4.20 A; A=1-1076.
DR PDBsum; 5B7I; -.
DR PDBsum; 5GQH; -.
DR AlphaFoldDB; Q02ML8; -.
DR SMR; Q02ML8; -.
DR DIP; DIP-61771N; -.
DR IntAct; Q02ML8; 1.
DR PRIDE; Q02ML8; -.
DR EnsemblBacteria; ABJ11601; ABJ11601; PA14_33340.
DR KEGG; pau:PA14_33340; -.
DR HOGENOM; CLU_009385_0_0_6; -.
DR OMA; VACHWIR; -.
DR BioCyc; PAER208963:G1G74-2806-MON; -.
DR Proteomes; UP000000653; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3210.30; -; 1.
DR InterPro; IPR006483; CRISPR-assoc_Cas3_HD.
DR InterPro; IPR038257; CRISPR-assoc_Cas3_HD_sf.
DR InterPro; IPR013395; Helicase_Cas3_CRISPR-ass_yers.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF18019; HD_6; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02562; cas3_yersinia; 1.
DR PROSITE; PS51643; HD_CAS3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; ATP-binding; Helicase; Hydrolase;
KW Magnesium; Metal-binding; Nucleotide-binding.
FT CHAIN 1..1076
FT /note="CRISPR-associated nuclease/helicase Cas3 subtype I-
FT F/YPEST"
FT /id="PRO_0000417605"
FT DOMAIN 102..318
FT /note="HD Cas3-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00974"
FT MOTIF 576..579
FT /note="DEAD box"
FT BINDING 124
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT MUTAGEN 124
FT /note="D->A: In a disruption mutant, does not restore
FT biofilm formation, restores crRNA production."
FT /evidence="ECO:0000269|PubMed:21398535"
FT MUTAGEN 576
FT /note="D->A: In a disruption mutant, does not restore
FT biofilm formation, restores crRNA production."
FT /evidence="ECO:0000269|PubMed:21398535"
FT STRAND 1..7
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 11..24
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 29..37
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 39..51
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 109..122
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 130..137
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 149..161
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 167..175
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 208..218
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 231..236
FT /evidence="ECO:0007829|PDB:5B7I"
FT TURN 237..240
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:5B7I"
FT TURN 246..249
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 271..285
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 290..298
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 301..320
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 349..366
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 370..373
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 381..384
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 393..412
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 414..418
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 426..437
FT /evidence="ECO:0007829|PDB:5B7I"
FT TURN 440..442
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 446..453
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 457..467
FT /evidence="ECO:0007829|PDB:5B7I"
FT TURN 471..473
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 474..479
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:5B7I"
FT TURN 522..526
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 529..531
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 532..538
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 540..545
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 546..549
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 551..554
FT /evidence="ECO:0007829|PDB:5B7I"
FT TURN 558..561
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 562..570
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 571..576
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 578..580
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 583..585
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 586..598
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 603..606
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 612..631
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 632..635
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 642..647
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 652..659
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 660..679
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 687..690
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 699..720
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 723..725
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 728..736
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 740..752
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 759..766
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 768..770
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 772..785
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 793..798
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 800..808
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 812..820
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 822..824
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 825..827
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 832..837
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 842..849
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 852..855
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 865..870
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 872..875
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 884..887
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 890..892
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 899..902
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 905..907
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 914..917
FT /evidence="ECO:0007829|PDB:5B7I"
FT TURN 925..927
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 929..940
FT /evidence="ECO:0007829|PDB:5B7I"
FT TURN 947..949
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 955..958
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 960..963
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 966..970
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 982..986
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 994..999
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 1001..1006
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 1008..1010
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 1011..1013
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 1022..1024
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 1030..1040
FT /evidence="ECO:0007829|PDB:5B7I"
FT HELIX 1045..1052
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 1064..1067
FT /evidence="ECO:0007829|PDB:5B7I"
FT TURN 1068..1070
FT /evidence="ECO:0007829|PDB:5B7I"
FT STRAND 1071..1074
FT /evidence="ECO:0007829|PDB:5B7I"
SQ SEQUENCE 1076 AA; 121091 MW; 8C66F4C5F622BB49 CRC64;
MNILLVSQCE KRALSETRRI LDQFAERRGE RTWQTPITQA GLDTLRRLLK KSARRNTAVA
CHWIRGRDHS ELLWIVGDAS RFNAQGAVPT NRTCRDILRK EDENDWHSAE DIRLLTVMAA
LFHDIGKASQ AFQAKLRNRG KPMADAYRHE WVSLRLFEAF VGPGSSDEDW LRRLADKRET
GDAWLSQLAR DDRQSAPPGP FQKSRLPPLA QAVGWLIVSH HRLPNGDHRG SASLARLPAP
IQSQWCGARD ADAKEKAACW QFPHGLPFAS AHWRARTALC AQSMLERPGL LARGPALLHD
SYVMHVSRLI LMLADHHYSS LPADSRLGDP NFPLHANTDR DSGKLKQRLD EHLLGVALHS
RKLAGTLPRL ERQLPRLARH KGFTRRVEQP RFRWQDKAYD CAMACREQAM EHGFFGLNLA
STGCGKTLAN GRILYALADP QRGARFSIAL GLRSLTLQTG QAYRERLGLG DDDLAILVGG
SAARELFEKQ QERLERSGSE SAQELLAENS HVHFAGTLED GPLREWLGRN SAGNRLLQAP
ILACTIDHLM PASESLRGGH QIAPLLRLMT SDLVLDEVDD FDIDDLPALS RLVHWAGLFG
SRVLLSSATL PPALVQGLFE AYRSGREIFQ RHRGAPGRAT EIRCAWFDEF SSQSSAHGAV
TSFSEAHATF VAQRLAKLEQ LPPRRQAQLC TVHAAGEARP ALCRELAGQM NTWMADLHRC
HHTEHQGRRI SFGLLRLANI EPLIELAQAI LAQGAPEGLH VHLCVYHSRH PLLVRSAIER
QLDELLKRSD DDAAALFARP TLAKALQAST ERDHLFVVLA SPVAEVGRDH DYDWAIVEPS
SMRSIIQLAG RIRRHRSGFS GEANLYLLSR NIRSLEGQNP AFQRPGFETP DFPLDSHDLH
DLLDPALLAR IDASPRIVEP FPLFPRSRLV DLEHRRLRAL MLADDPPSSL LGVPLWWQTP
ASLSGALQTS QPFRAGAKER CYALLPDEDD EERLHFSRYE EGTWSNQDNL LRNLDLTYGP
RIQTWGTVNY REELVAMAGR EDLDLRQCAM RYGEVRLREN TQGWSYHPYL GFKKYN
