CAS1_PECAS
ID CAS1_PECAS Reviewed; 326 AA.
AC Q6D0X0;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=CRISPR-associated endonuclease Cas1 {ECO:0000255|HAMAP-Rule:MF_01470};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01470};
GN Name=cas1 {ECO:0000255|HAMAP-Rule:MF_01470}; OrderedLocusNames=ECA3679;
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 CAS3, 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). Acts as
CC a dsDNA endonuclease. Involved in the integration of spacer DNA into
CC the CRISPR cassette (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:23637624}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01470};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01470};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with Cas3, in the absence
CC of crRNA. {ECO:0000250, 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 {ECO:0000269|PubMed:23637624}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated endonuclease Cas1 family.
CC {ECO:0000255|HAMAP-Rule:MF_01470}.
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DR EMBL; BX950851; CAG76577.1; -; Genomic_DNA.
DR RefSeq; WP_011095179.1; NC_004547.2.
DR PDB; 5FCL; X-ray; 2.70 A; A/B/C/D/E/F=1-326.
DR PDBsum; 5FCL; -.
DR AlphaFoldDB; Q6D0X0; -.
DR SMR; Q6D0X0; -.
DR STRING; 218491.ECA3679; -.
DR EnsemblBacteria; CAG76577; CAG76577; ECA3679.
DR KEGG; eca:ECA3679; -.
DR eggNOG; COG1518; Bacteria.
DR HOGENOM; CLU_074119_0_0_6; -.
DR OMA; YYLQHCR; -.
DR OrthoDB; 1581397at2; -.
DR Proteomes; UP000007966; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004520; F:endodeoxyribonuclease activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-UniRule.
DR GO; GO:0043571; P:maintenance of CRISPR repeat elements; IEA:UniProtKB-UniRule.
DR CDD; cd09718; Cas1_I-F; 1.
DR Gene3D; 1.20.120.920; -; 1.
DR Gene3D; 3.100.10.20; -; 1.
DR HAMAP; MF_01470; Cas1; 1.
DR InterPro; IPR002729; CRISPR-assoc_Cas1.
DR InterPro; IPR042206; CRISPR-assoc_Cas1_C.
DR InterPro; IPR042211; CRISPR-assoc_Cas1_N.
DR InterPro; IPR019857; CRISPR-assoc_Cas1_YPEST-subtyp.
DR Pfam; PF01867; Cas_Cas1; 1.
DR TIGRFAMs; TIGR00287; cas1; 1.
DR TIGRFAMs; TIGR03637; cas1_YPEST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; DNA-binding; Endonuclease; Hydrolase;
KW Magnesium; Manganese; Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1..326
FT /note="CRISPR-associated endonuclease Cas1"
FT /id="PRO_0000430240"
FT BINDING 191
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01470"
FT BINDING 255
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01470"
FT BINDING 269
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01470"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:5FCL"
FT TURN 17..20
FT /evidence="ECO:0007829|PDB:5FCL"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:5FCL"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:5FCL"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:5FCL"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:5FCL"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:5FCL"
FT HELIX 69..78
FT /evidence="ECO:0007829|PDB:5FCL"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:5FCL"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:5FCL"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:5FCL"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:5FCL"
FT HELIX 127..150
FT /evidence="ECO:0007829|PDB:5FCL"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:5FCL"
FT HELIX 164..180
FT /evidence="ECO:0007829|PDB:5FCL"
FT HELIX 184..205
FT /evidence="ECO:0007829|PDB:5FCL"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:5FCL"
FT HELIX 222..245
FT /evidence="ECO:0007829|PDB:5FCL"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:5FCL"
FT HELIX 262..268
FT /evidence="ECO:0007829|PDB:5FCL"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:5FCL"
FT HELIX 272..286
FT /evidence="ECO:0007829|PDB:5FCL"
FT HELIX 290..304
FT /evidence="ECO:0007829|PDB:5FCL"
FT HELIX 306..321
FT /evidence="ECO:0007829|PDB:5FCL"
SQ SEQUENCE 326 AA; 36258 MW; 628C37C0FD0C7F87 CRC64;
MDNAFSPSDL KTILHSKRAN VYYLQHCRIL VNGGRVEYVT EEGNQSLYWN IPIANTSVVM
LGTGTSVTQA AMREFARAGV MIGFCGGGGT PLFAANEAEV AVSWLSPQSE YRPTEYLQDW
VSFWFDDEKR LAAAIAFQQV RITQIRQHWL GSRLSRESRF TFKSEHLQAL LDRYQKGLTD
CRTSNDVLVQ EAMMTKALYR LAANAVSYGD FTRAKRGGGT DLANRFLDHG NYLAYGLAAV
STWVLGLPHG LAVLHGKTRR GGLVFDVADL IKDALVLPQA FIAAMEGEDE QEFRQRCLTA
FQQSEALDVM IGSLQDVASK LSQVVR
