ID A7ZQJ8_ECO24 Unreviewed; 306 AA.
AC A7ZQJ8;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 76.
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 ECO:0000313|EMBL:ABV17143.1};
GN OrderedLocusNames=EcE24377A_3057 {ECO:0000313|EMBL:ABV17143.1};
OS Escherichia coli O139:H28 (strain E24377A / ETEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=331111 {ECO:0000313|EMBL:ABV17143.1, ECO:0000313|Proteomes:UP000001122};
RN [1] {ECO:0000313|Proteomes:UP000001122}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E24377A / ETEC {ECO:0000313|Proteomes:UP000001122};
RX PubMed=18676672; DOI=10.1128/JB.00619-08;
RA Rasko D.A., Rosovitz M.J., Myers G.S., Mongodin E.F., Fricke W.F.,
RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA Henderson I.R., Sperandio V., Ravel J.;
RT "The pangenome structure of Escherichia coli: comparative genomic analysis
RT of E. coli commensal and pathogenic isolates.";
RL J. Bacteriol. 190:6881-6893(2008).
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|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; CP000800; ABV17143.1; -; Genomic_DNA.
DR RefSeq; WP_000144881.1; NC_009801.1.
DR AlphaFoldDB; A7ZQJ8; -.
DR KEGG; ecw:EcE24377A_3057; -.
DR HOGENOM; CLU_077904_1_0_6; -.
DR Proteomes; UP000001122; 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; cd09719; Cas1_I-E; 1.
DR Gene3D; 1.20.120.920; CRISPR-associated endonuclease Cas1, C-terminal domain; 1.
DR Gene3D; 3.100.10.20; CRISPR-associated endonuclease Cas1, N-terminal domain; 1.
DR HAMAP; MF_01470; Cas1; 1.
DR InterPro; IPR033641; Cas1_I-E.
DR InterPro; IPR002729; CRISPR-assoc_Cas1.
DR InterPro; IPR042206; CRISPR-assoc_Cas1_C.
DR InterPro; IPR019851; CRISPR-assoc_Cas1_ECOLI.
DR InterPro; IPR042211; CRISPR-assoc_Cas1_N.
DR NCBIfam; TIGR00287; cas1; 2.
DR NCBIfam; TIGR03638; cas1_ECOLI; 1.
DR PANTHER; PTHR34353:SF3; CRISPR-ASSOCIATED ENDONUCLEASE CAS1; 1.
DR PANTHER; PTHR34353; 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|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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001122}.
FT REGION 278..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 141
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
FT BINDING 208
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
FT BINDING 221
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
SQ SEQUENCE 306 AA; 33396 MW; 69ADBB6B2D467340 CRC64;
MTFVPLSPIP LKDRTTMIFL QYGQIDVLDG AFVLIDKTGI RTHIPVGSVA CIMLEPGTRV
SHAAVHLAAT VGTLLVWVGE AGVRVYSSGQ PGGARADKLL YQAKLALTED LRLKVVRKMY
ELRFREPPPA RRSVEQLRGI EGSRVRQTYA LLAKQYGVKW NGRKYDPKDW EKGDVVNRCI
SAATSCLYGI SEAAVLAAGY APAIGFIHSG KPLSFVYDIA DIIKFDSVVP KAFEIAARQP
AEPDKEVRLA CRDIFRSTKL TGKLIPLIEE VLAAGEIEPP QPAPDMLPPA IPEPETLGDS
GHRGRG
//
