ID   CAS3_PECAS              Reviewed;        1098 AA.
AC   Q6D0W9;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=ECA3680;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
RN   [2]
RP   INDUCTION, AND OPERON STRUCTURE.
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=21519197; DOI=10.4161/rna.8.3.15190;
RA   Przybilski R., Richter C., Gristwood T., Clulow J.S., Vercoe R.B.,
RA   Fineran P.C.;
RT   "Csy4 is responsible for CRISPR RNA processing in Pectobacterium
RT   atrosepticum.";
RL   RNA Biol. 8:517-528(2011).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CAS1, AND SUBUNIT.
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=23226499; DOI=10.1371/journal.pone.0049549;
RA   Richter C., Gristwood T., Clulow J.S., Fineran P.C.;
RT   "In vivo protein interactions and complex formation in the Pectobacterium
RT   atrosepticum subtype I-F CRISPR/Cas System.";
RL   PLoS ONE 7:E49549-E49549(2012).
RN   [4]
RP   FUNCTION, AND BIOTECHNOLOGY.
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=23637624; DOI=10.1371/journal.pgen.1003454;
RA   Vercoe R.B., Chang J.T., Dy R.L., Taylor C., Gristwood T., Clulow J.S.,
RA   Richter C., Przybilski R., Pitman A.R., Fineran P.C.;
RT   "Cytotoxic chromosomal targeting by CRISPR/Cas systems can reshape
RT   bacterial genomes and expel or remodel pathogenicity islands.";
RL   PLoS Genet. 9:E1003454-E1003454(2013).
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). Might
CC       be involved in the integration of spacer DNA into the CRISPR cassette.
CC       {ECO:0000269|PubMed:23637624}.
CC   -!- SUBUNIT: Interacts with Cas1 in the absence of crRNA. Probably
CC       interacts with the Csy ribonucleoprotein complex composed of cys1,
CC       cys2, csy3, cas6f and crRNA. {ECO:0000269|PubMed:23226499}.
CC   -!- INDUCTION: Expressed in late exponential phase (other phases not
CC       tested); part of a large cas-CRISPR3 polycistronic operon.
CC       {ECO:0000269|PubMed:21519197}.
CC   -!- BIOTECHNOLOGY: If the spacer DNA has a perfect match in the chromosome
CC       then toxicity results. Suppression of the toxic effects occurs via
CC       mutations in the CRISPR/Cas machinery, or via target deletion, which
CC       might contribute to genome plasticity. This CRISPR/Cas system can be
CC       used to remove genomic islands, and possibly other genomic regions
CC       (PubMed:23637624). {ECO:0000269|PubMed:23637624}.
CC   -!- MISCELLANEOUS: The N-terminus (1-about 100) might be the equivalent of
CC       Cas2 in this CRISPR subtype.
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; BX950851; CAG76578.1; -; Genomic_DNA.
DR   RefSeq; WP_011095180.1; NC_004547.2.
DR   AlphaFoldDB; Q6D0W9; -.
DR   SMR; Q6D0W9; -.
DR   STRING; 218491.ECA3680; -.
DR   EnsemblBacteria; CAG76578; CAG76578; ECA3680.
DR   KEGG; eca:ECA3680; -.
DR   PATRIC; fig|218491.5.peg.3732; -.
DR   eggNOG; COG1203; Bacteria.
DR   HOGENOM; CLU_009385_0_0_6; -.
DR   OMA; VACHWIR; -.
DR   OrthoDB; 1149839at2; -.
DR   Proteomes; UP000007966; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004518; F:nuclease activity; 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   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR02562; cas3_yersinia; 1.
DR   PROSITE; PS51643; HD_CAS3; 1.
PE   1: Evidence at protein level;
KW   Antiviral defense; ATP-binding; Helicase; Hydrolase; Magnesium;
KW   Metal-binding; Nuclease; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..1098
FT                   /note="CRISPR-associated nuclease/helicase Cas3 subtype I-
FT                   F/YPEST"
FT                   /id="PRO_0000430241"
FT   DOMAIN          102..327
FT                   /note="HD Cas3-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00974"
FT   REGION          497..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           591..594
FT                   /note="DEAD box"
FT   COMPBIAS        504..519
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         124
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255"
FT   BINDING         216
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1098 AA;  124892 MW;  95DC886E1AF4C5A0 CRC64;
     MNILLISECN KRALVETRRI LDQFAERKGE RSWQTAITLE GLNTLRKLLR KTARRNTAVA
     CHWIRSTNHT ELLWVVGNLR RFNAQGSVPT NTTSRDVLRT KDENPWHSAE VFSLLAAIAG
     LFHDVGKANA LFQAGLSGTG PRSQPYRHEW VSLRLFQAFV GEQDDKAWLT TLSMITSEAE
     VALLATLQQD KPTFSDSPFR TLPPLAQTIA WLIVSHHRLP VFNKSTELAP NSSEPQLSFA
     ETWLTDHLSP QWNALNHCQI GWTPHEREQN WQFPNGTPLY SAVWREKARK FAGRALKLPS
     FMHFSQLDQR LTVHLARLAL MLADHHYSAG AATVGWQDIT YPVWANTDRK TGEYKQRLDE
     HCVGVGQNAL LLGRSLPHLR DTLPAITRHK GFRQRSTHPR FRWQDRAFDL ACSIRETSKQ
     HGFFGINMAS TGRGKTFANA RIMYGLSDES TGCRFSVALG LRTLTLQTGD ALRQRLKLDE
     DDLAVLIGSQ AVQDLHEMRK ENQQRQQNTP QTGSESADPL FSEHQYVRYD GSLDDGRLKA
     WLERSPTLHQ LLSAPVLITT IDHLMPATEA LRGGHQIAPM LRLLTADLVL DEPDDFGLED
     LPALCRLVNW AGMLGSRVLL SSATLPPALI RALFDAYLDG RTAWQQAYGT PNTPLNVCCG
     WFDEFDCQHE QYGDVKDFMV RHDAFVHQRL KNLTKDELPL RFATIVPVSS PSKNADDVYL
     AVAQAIHPRM FDLHSQHHQQ HENGKTVSLG LVRMANIDPL VAVARQLLAI PSPPDTCIHY
     CIYHSQHPLA MRSHIEQRLD AALMRNDADA LWQVEEIRQA IEKSSQRHHV FVALATSVAE
     VGRDHDYDWA IVEPSSMRSL IQPAGRILRH RQDKQYVPKT PNIYLLSHNI RALRGKDIAY
     CKPGFESQDD SLDTHDLHQL LQEKEYRHLS AAPRIVQPMS FAKPLSLVAL EHAVLGKTLL
     GLKNKKLDDL KRPPAAFWWR AHPHWNGELQ RRTPFRQSAK DEAYTLWIAD DDEEPVFMVQ
     DDGPSGWKQS DIARPVTLNM AEGVSAWIEP DYHALYQQLA EEKQWELSWV SARFGEIRLR
     EEEDWYWHPL LGVFGALS