ID D3HLI6_LEGLN Unreviewed; 979 AA.
AC D3HLI6;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN OrderedLocusNames=LLO_2867 {ECO:0000313|EMBL:CBJ13306.1};
OS Legionella longbeachae serogroup 1 (strain NSW150).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=661367 {ECO:0000313|EMBL:CBJ13306.1, ECO:0000313|Proteomes:UP000001060};
RN [1] {ECO:0000313|EMBL:CBJ13306.1, ECO:0000313|Proteomes:UP000001060}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSW150 {ECO:0000313|EMBL:CBJ13306.1,
RC ECO:0000313|Proteomes:UP000001060};
RX PubMed=20174605; DOI=10.1371/journal.pgen.1000851;
RA Cazalet C., Gomez-Valero L., Rusniok C., Lomma M., Dervins-Ravault D.,
RA Newton H., Sansom F., Jarraud S., Zidane N., Ma L., Bouchier C.,
RA Etienne J., Hartland E., Buchrieser C.;
RT "Analysis of the Legionella longbeachae genome and transcriptome uncovers
RT unique strategies to cause Legionnaires' disease.";
RL PLoS Genet. 6:E1000851-E1000851(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of DNA to give random double-stranded
CC fragments with terminal 5'-phosphates, ATP is simultaneously
CC hydrolyzed.; EC=3.1.21.3; Evidence={ECO:0000256|ARBA:ARBA00000851};
CC -!- SIMILARITY: Belongs to the HsdR family.
CC {ECO:0000256|ARBA:ARBA00008598}.
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DR EMBL; FN650140; CBJ13306.1; -; Genomic_DNA.
DR RefSeq; WP_012979396.1; NC_013861.1.
DR AlphaFoldDB; D3HLI6; -.
DR STRING; 661367.LLO_2867; -.
DR REBASE; 24304; LloNSWORF2865P.
DR KEGG; llo:LLO_2867; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_010804_0_0_6; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000001060; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009035; F:type I site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR CDD; cd22332; HsdR_N; 1.
DR Gene3D; 3.90.1570.50; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N.
DR InterPro; IPR040980; SWI2_SNF2.
DR PANTHER; PTHR42927; HELICASE SUPERFAMILY 1 AND 2 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR42927:SF1; HELICASE SUPERFAMILY 1 AND 2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF04313; HSDR_N; 1.
DR Pfam; PF18766; SWI2_SNF2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001060};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 289..482
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 979 AA; 111299 MW; EFAF8EF5F1FCD343 CRC64;
MKFTNTSEGG FETTIVNSLL QEAGYKAGNP QDYERSHAID LKKLSDFLQA TQPEIAEGLN
LSVDSPKRTT FLHRLQGEIA KHGIINILRK GIKHGPDTIT LFYGSPTENN TKAKAMFEQN
LFSVTRQLRY SSNETQLALD MAIFINGLPI VTFELKNKLT KQTVEDAVQQ YKNDRDPKEL
LFQFGRCLVH FAVDDHEVRM CTHLKGKSSW FLPFNKGFKD GAGNPPNPEG LATDYLWKEI
LTPDRLTDII ENYAQIIEEK DEKTGKKKFK QIFPRYHQLT VVRKLLESVQ IHGAGKRYLI
QHSAGSGKSN SIAWLAHQLV GLEQNKQAVF DSILVVTDRR ILDKQIRDSI KSFAQVSSIV
GHAERSGDLR RFITEGKKII ITTVQKFPFI LSEIGNEHRQ NKFAIIIDEA HSSQSGKTAS
KMNMALSENV SESDEDSTED KINELMESRK MLTNASYFAF TATPKNKTLE IFGEPEPQPD
GRIKHHPFHS YTMKQAIQEG FILDVLKNYT PVASFYRLTK AVEGDPLFDT KKAQKKLRKY
VESNTHAIRE KAEIMIDHFH THIMGQRKIG GSARAMIVTS GISRAIEYFH AVNDYLKERN
LPYKSIVAFS GEHEYGGQKV TEASLNGFPS NLIGEKIAED PYRLLVVADK FLTGYDEPLM
HTMYVDKPLS GIKAVQTLSR LNRAHPKKYD TFVLDFYNDV DTIEKSFSDY YRTTILSEET
DPNKLHDLQS DLDGYQVYSA EQIHQLAERY LNGADREKLD PILDNCVAVY NNELDEDGQV
DFKGKAKAFI RTYGFLSSIL PYNYAEWEKL SIFLNFLVPK LPTPKEEDHS IGILETIDMD
SYRAEVQASI NIRLADEDAE LDAVPTSAGG RKAEPEMDQL SNIIRVFNDL FGNIEWKDGD
KIRQIITEEI PGKVASDSAY QNAMKNSDRH NARIEHDRAL ARVMVELIAD HTELYKQFSD
NPSFKKWLGD TIFGATYQK
//
