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Database: UniProt
Entry: S5R0U9_9STRE
LinkDB: S5R0U9_9STRE
Original site: S5R0U9_9STRE 
ID   S5R0U9_9STRE            Unreviewed;       288 AA.
AC   S5R0U9;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=CRISPR-associated endonuclease Cas1 {ECO:0000256|HAMAP-Rule:MF_01470};
DE            EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01470};
GN   Name=cas1 {ECO:0000256|HAMAP-Rule:MF_01470};
GN   ORFNames=KE3_1336 {ECO:0000313|EMBL:AGS05814.1};
OS   Streptococcus lutetiensis 033.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1076934 {ECO:0000313|EMBL:AGS05814.1, ECO:0000313|Proteomes:UP000015268};
RN   [1] {ECO:0000313|EMBL:AGS05814.1, ECO:0000313|Proteomes:UP000015268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=033 {ECO:0000313|EMBL:AGS05814.1,
RC   ECO:0000313|Proteomes:UP000015268};
RX   PubMed=23782707; DOI=10.1186/1471-2180-13-141;
RA   Jin D., Chen C., Li L., Lu S., Li Z., Zhou Z., Jing H., Xu Y., Du P.,
RA   Wang H., Xiong Y., Zheng H., Bai X., Sun H., Wang L., Ye C., Gottschalk M.,
RA   Xu J.;
RT   "Dynamics of fecal microbial communities in children with diarrhea of
RT   unknown etiology and genomic analysis of associated Streptococcus
RT   lutetiensis.";
RL   BMC Microbiol. 13:141-141(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 spacers, 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. {ECO:0000256|HAMAP-Rule:MF_01470}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01470};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01470};
CC   -!- SUBUNIT: Homodimer, forms a heterotetramer with a Cas2 homodimer.
CC       {ECO:0000256|ARBA:ARBA00038592, ECO:0000256|HAMAP-Rule:MF_01470}.
CC   -!- SIMILARITY: Belongs to the CRISPR-associated endonuclease Cas1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01470}.
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DR   EMBL; CP003025; AGS05814.1; -; Genomic_DNA.
DR   RefSeq; WP_020917063.1; NC_021900.1.
DR   AlphaFoldDB; S5R0U9; -.
DR   KEGG; slu:KE3_1336; -.
DR   PATRIC; fig|1076934.5.peg.1298; -.
DR   HOGENOM; CLU_055263_1_0_9; -.
DR   Proteomes; UP000015268; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004520; F:DNA endonuclease 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; cd09720; Cas1_II; 1.
DR   Gene3D; 1.20.120.920; CRISPR-associated endonuclease Cas1, C-terminal domain; 1.
DR   HAMAP; MF_01470; Cas1; 1.
DR   InterPro; IPR002729; CRISPR-assoc_Cas1.
DR   InterPro; IPR042206; CRISPR-assoc_Cas1_C.
DR   InterPro; IPR019855; CRISPR-assoc_Cas1_NMENI.
DR   NCBIfam; TIGR00287; cas1; 1.
DR   NCBIfam; TIGR03639; cas1_NMENI; 1.
DR   PANTHER; PTHR34353; CRISPR-ASSOCIATED ENDONUCLEASE CAS1 1; 1.
DR   PANTHER; PTHR34353:SF2; CRISPR-ASSOCIATED ENDONUCLEASE CAS1 1; 1.
DR   Pfam; PF01867; Cas_Cas1; 1.
PE   3: Inferred from homology;
KW   Antiviral defense {ECO:0000256|ARBA:ARBA00023118, ECO:0000256|HAMAP-
KW   Rule:MF_01470};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_01470};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW   Rule:MF_01470};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01470};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01470};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01470};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01470};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01470}.
FT   BINDING         148
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
FT   BINDING         204
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
FT   BINDING         219
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
SQ   SEQUENCE   288 AA;  33786 MW;  69F3326FC14B79FF CRC64;
     MGWRTVIVNE HSKLSYKNNH LIFKDAYHTE MIHLEEIDIL LLETTNIILT TMLIERLVDR
     NILIIFCDEK RLPTAMLTPY YGRHDSSLQL TNQIAWDDEV KCDVWTNIIA QKILNQSMYL
     GECSYFEKSQ SIMDLYHGLE PFDPSNREGH SARIYFNTLF GNDFSREQDN DINAGLDYGY
     TLLLSMFARE LVVCGCMTQF GLKHSNQFNQ FNLASDIMEP FRPIVDRIVY ENRNASFVKI
     KRELFTMFDE TYSYNNKEMY LNNIVSDYTK KVVKALNHNG KGVPEFRI
//
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