CAS1_PSEAB
ID CAS1_PSEAB Reviewed; 324 AA.
AC Q02ML7;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=CRISPR-associated endonuclease Cas1;
DE EC=3.1.-.-;
GN Name=cas1; OrderedLocusNames=PA14_33350;
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 X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS) IN COMPLEX WITH MANGANESE, FUNCTION
RP AS DNA ENDONUCLEASE, COFACTOR, ACTIVITY REGULATION, SUBUNIT, AND
RP MUTAGENESIS OF GLU-190; ASN-223; HIS-254; ASP-265 AND ASP-268.
RC STRAIN=UCBPP-PA14;
RX PubMed=19523907; DOI=10.1016/j.str.2009.03.019;
RA Wiedenheft B., Zhou K., Jinek M., Coyle S.M., Ma W., Doudna J.A.;
RT "Structural basis for DNase activity of a conserved protein implicated in
RT CRISPR-mediated genome defense.";
RL Structure 17:904-912(2009).
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).
CC Involved in the integration of spacer DNA into the CRISPR cassette (By
CC similarity). Acts as a ss- and dsDNA-specific endonuclease
CC (PubMed:19523907). {ECO:0000255|HAMAP-Rule:MF_01470,
CC ECO:0000269|PubMed:19523907}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01470,
CC ECO:0000269|PubMed:19523907};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01470,
CC ECO:0000269|PubMed:19523907};
CC Note=Mn(2+) supports cleavage of ss- and dsDNA, while Mg(2+) only
CC supports digestion of dsDNA in vitro. {ECO:0000269|PubMed:19523907};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:19523907}.
CC -!- SUBUNIT: Homodimer (PubMed:19523907). This bacteria does not encode
CC Cas2; Cas1 must interact with a different protein to insert spacers
CC (Probable). {ECO:0000305, ECO:0000305|PubMed:19523907}.
CC -!- INTERACTION:
CC Q02ML7; Q02ML7: cas1; NbExp=2; IntAct=EBI-15788664, EBI-15788664;
CC -!- SIMILARITY: Belongs to the CRISPR-associated endonuclease Cas1 family.
CC {ECO:0000305}.
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DR EMBL; CP000438; ABJ11600.1; -; Genomic_DNA.
DR RefSeq; WP_003139228.1; NZ_CP034244.1.
DR PDB; 3GOD; X-ray; 2.17 A; A/B/C/D=1-324.
DR PDBsum; 3GOD; -.
DR AlphaFoldDB; Q02ML7; -.
DR SMR; Q02ML7; -.
DR DIP; DIP-48307N; -.
DR PRIDE; Q02ML7; -.
DR EnsemblBacteria; ABJ11600; ABJ11600; PA14_33350.
DR KEGG; pau:PA14_33350; -.
DR HOGENOM; CLU_074119_0_0_6; -.
DR OMA; YYLQHCR; -.
DR BioCyc; PAER208963:G1G74-2807-MON; -.
DR EvolutionaryTrace; Q02ML7; -.
DR Proteomes; UP000000653; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004520; F:endodeoxyribonuclease activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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.
FT CHAIN 1..324
FT /note="CRISPR-associated endonuclease Cas1"
FT /id="PRO_0000417082"
FT BINDING 190
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:19523907,
FT ECO:0007744|PDB:3GOD"
FT BINDING 254
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:19523907,
FT ECO:0007744|PDB:3GOD"
FT BINDING 268
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:19523907,
FT ECO:0007744|PDB:3GOD"
FT MUTAGEN 190
FT /note="E->A: Protein is unstable."
FT /evidence="ECO:0000269|PubMed:19523907"
FT MUTAGEN 223
FT /note="N->A: Slight decrease in endonuclease activity."
FT /evidence="ECO:0000269|PubMed:19523907"
FT MUTAGEN 254
FT /note="H->A: Protein is unstable."
FT /evidence="ECO:0000269|PubMed:19523907"
FT MUTAGEN 265
FT /note="D->A: Considerable decrease in endonuclease
FT activity."
FT /evidence="ECO:0000269|PubMed:19523907"
FT MUTAGEN 268
FT /note="D->A: Almost complete loss of endonuclease
FT activity."
FT /evidence="ECO:0000269|PubMed:19523907"
FT HELIX 6..15
FT /evidence="ECO:0007829|PDB:3GOD"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:3GOD"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:3GOD"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:3GOD"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:3GOD"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:3GOD"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:3GOD"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:3GOD"
FT HELIX 68..76
FT /evidence="ECO:0007829|PDB:3GOD"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:3GOD"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:3GOD"
FT STRAND 97..109
FT /evidence="ECO:0007829|PDB:3GOD"
FT HELIX 114..123
FT /evidence="ECO:0007829|PDB:3GOD"
FT HELIX 126..150
FT /evidence="ECO:0007829|PDB:3GOD"
FT HELIX 152..156
FT /evidence="ECO:0007829|PDB:3GOD"
FT HELIX 163..178
FT /evidence="ECO:0007829|PDB:3GOD"
FT HELIX 183..204
FT /evidence="ECO:0007829|PDB:3GOD"
FT HELIX 221..243
FT /evidence="ECO:0007829|PDB:3GOD"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:3GOD"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:3GOD"
FT HELIX 261..267
FT /evidence="ECO:0007829|PDB:3GOD"
FT TURN 268..274
FT /evidence="ECO:0007829|PDB:3GOD"
FT HELIX 275..285
FT /evidence="ECO:0007829|PDB:3GOD"
FT HELIX 289..302
FT /evidence="ECO:0007829|PDB:3GOD"
FT HELIX 305..319
FT /evidence="ECO:0007829|PDB:3GOD"
SQ SEQUENCE 324 AA; 36106 MW; 1DAC69463D30681D CRC64;
MDDISPSELK TILHSKRANL YYLQHCRVLV NGGRVEYVTD EGRHSHYWNI PIANTTSLLL
GTGTSITQAA MRELARAGVL VGFCGGGGTP LFSANEVDVE VSWLTPQSEY RPTEYLQRWV
GFWFDEEKRL VAARHFQRAR LERIRHSWLE DRVLRDAGFA VDATALAVAV EDSARALEQA
PNHEHLLTEE ARLSKRLFKL AAQATRYGEF VRAKRGSGGD PANRFLDHGN YLAYGLAATA
TWVLGIPHGL AVLHGKTRRG GLVFDVADLI KDSLILPQAF LSAMRGDEEQ DFRQACLDNL
SRAQALDFMI DTLKDVAQRS TVSA
