ID D8L2S0_KLEPN Unreviewed; 1094 AA.
AC D8L2S0;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Type I restriction enzyme endonuclease subunit {ECO:0000256|RuleBase:RU364115};
DE Short=R protein {ECO:0000256|RuleBase:RU364115};
DE EC=3.1.21.3 {ECO:0000256|RuleBase:RU364115};
GN Name=hsdR {ECO:0000313|EMBL:ADJ18715.1};
GN Synonyms=hsdR_10 {ECO:0000313|EMBL:STV75587.1};
GN ORFNames=NCTC13443_07328 {ECO:0000313|EMBL:STV75587.1};
OS Klebsiella pneumoniae.
OG Plasmid PU25001 {ECO:0000313|EMBL:ALI93314.1},
OG Plasmid p1220-CTXM {ECO:0000313|EMBL:ASF89751.1},
OG Plasmid pKP048 {ECO:0000313|EMBL:ADJ18715.1}, and
OG Plasmid pKp848CTX {ECO:0000313|EMBL:CDY80154.1}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573 {ECO:0000313|EMBL:ADJ18715.1};
RN [1] {ECO:0000313|EMBL:ADJ18715.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KP048 {ECO:0000313|EMBL:ADJ18715.1};
RC PLASMID=pKP048 {ECO:0000313|EMBL:ADJ18715.1};
RX PubMed=19620332; DOI=10.1128/AAC.00260-09;
RA Shen P., Wei Z., Jiang Y., Du X., Ji S., Yu Y., Li L.;
RT "Novel genetic environment of the carbapenem-hydrolyzing beta-lactamase
RT KPC-2 among Enterobacteriaceae in China.";
RL Antimicrob. Agents Chemother. 53:4333-4338(2009).
RN [2] {ECO:0000313|EMBL:ADJ18715.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KP048 {ECO:0000313|EMBL:ADJ18715.1};
RC PLASMID=pKP048 {ECO:0000313|EMBL:ADJ18715.1};
RX PubMed=20547789; DOI=10.1128/AAC.00137-10;
RA Jiang Y., Yu D., Wei Z., Shen P., Zhou Z., Yu Y.;
RT "Complete nucleotide sequence of Klebsiella pneumoniae multidrug resistance
RT plasmid pKP048, carrying blaKPC-2, blaDHA-1, qnrB4, and armA.";
RL Antimicrob. Agents Chemother. 54:3967-3969(2010).
RN [3] {ECO:0000313|EMBL:CDY80154.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST17 Kp848 {ECO:0000313|EMBL:CDY80154.1};
RC PLASMID=pKp848CTX {ECO:0000313|EMBL:CDY80154.1};
RX PubMed=25738592; DOI=10.1371/journal.pone.0116516;
RA Lohr I.H., Hulter N., Bernhoff E., Johnsen P.J., Sundsfjord A., Naseer U.;
RT "Persistence of a pKPN3-Like CTX-M-15-Encoding IncFIIK Plasmid in a
RT Klebsiella pneumonia ST17 Host during Two Years of Intestinal
RT Colonization.";
RL PLoS ONE 10:e0116516-e0116516(2015).
RN [4] {ECO:0000313|EMBL:ALI93314.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=U25 {ECO:0000313|EMBL:ALI93314.1};
RC PLASMID=PU25001 {ECO:0000313|EMBL:ALI93314.1};
RX PubMed=26872343; DOI=10.1590/0074-02760150423;
RA Rafiq Z., Sam N., Vaidyanathan R.;
RT "Whole genome sequence of Klebsiella pneumoniae U25, a hypermucoviscous,
RT multidrug resistant, biofilm producing isolate from India.";
RL Mem. Inst. Oswaldo Cruz 111:144-146(2016).
RN [5] {ECO:0000313|EMBL:ASF89751.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=1220 {ECO:0000313|EMBL:ASF89751.1};
RC PLASMID=p1220-CTXM {ECO:0000313|EMBL:ASF89751.1};
RX PubMed=28799786; DOI=.2217/fmb-2017-0026;
RA Zhang D., Yin Z., Zhao Y., Feng J., Jiang X., Zhan Z., Wu W., Chen W.,
RA Wang J., Li J., Zhou D.;
RT "p1220-CTXM, a pKP048-related IncFIIK plasmid carrying bla CTX-M-14 and
RT qnrB4.";
RL Future Microbiol. 12:1035-1043(2017).
RN [6] {ECO:0000313|EMBL:STV75587.1, ECO:0000313|Proteomes:UP000255518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13443 {ECO:0000313|EMBL:STV75587.1,
RC ECO:0000313|Proteomes:UP000255518};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Subunit R is required for both nuclease and ATPase
CC activities, but not for modification. {ECO:0000256|RuleBase:RU364115}.
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 ECO:0000256|RuleBase:RU364115};
CC -!- SUBUNIT: The type I restriction/modification system is composed of
CC three polypeptides R, M and S. {ECO:0000256|RuleBase:RU364115}.
CC -!- SIMILARITY: Belongs to the HsdR family. {ECO:0000256|ARBA:ARBA00008598,
CC ECO:0000256|RuleBase:RU364115}.
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DR EMBL; FJ628167; ADJ18715.1; -; Genomic_DNA.
DR EMBL; KT203286; ALI93314.1; -; Genomic_DNA.
DR EMBL; KY174332; ASF89751.1; -; Genomic_DNA.
DR EMBL; LM994717; CDY80154.1; -; Genomic_DNA.
DR EMBL; UGKT01000003; STV75587.1; -; Genomic_DNA.
DR RefSeq; WP_013214044.1; NZ_WUMA01000058.1.
DR RefSeq; YP_003754141.1; NC_014312.1.
DR RefSeq; YP_009062426.1; NC_024992.1.
DR REBASE; 26888; KpnKP048ORFBP.
DR PATRIC; fig|573.1365.peg.4429; -.
DR Proteomes; UP000255518; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; 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 GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd18030; DEXHc_RE_I_HsdR; 1.
DR CDD; cd22332; HsdR_N; 1.
DR CDD; cd18800; SF2_C_EcoR124I-like; 1.
DR Gene3D; 3.90.1570.50; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N.
DR InterPro; IPR004473; Restrct_endonuc_typeI_HsdR.
DR InterPro; IPR040980; SWI2_SNF2.
DR NCBIfam; TIGR00348; hsdR; 1.
DR PANTHER; PTHR30195:SF15; TYPE I RESTRICTION ENYME HINDI ENDONUCLEASE SUBUNIT; 1.
DR PANTHER; PTHR30195; TYPE I SITE-SPECIFIC DEOXYRIBONUCLEASE PROTEIN SUBUNIT M AND R; 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, ECO:0000256|RuleBase:RU364115};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU364115};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Helicase {ECO:0000313|EMBL:ALI93314.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364115};
KW Methyltransferase {ECO:0000313|EMBL:ASF89751.1};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364115}; Plasmid {ECO:0000313|EMBL:ADJ18715.1};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}; Transferase {ECO:0000313|EMBL:ASF89751.1}.
FT DOMAIN 334..503
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1094 AA; 124048 MW; BE0422E158F01136 CRC64;
MNQTYTPKFQ EEYSAKIPAL TLLTSLGWTF LSPKQIMDYR GYKQDEVVLR PVLREELSKR
SFMAGGKTCQ LSEKALDNLI SQVCSPALNE GLLKANERMY NHLLYGIAVT EFVDGKKVNP
TIALIDWEHP ENNQFHFTEE FTVLRSGGVE TRRPDIVCFV NGIPLAVIEA KSPAGHGKKG
PTIDEGISQS IRNQLNDEIP QLFVYSQLLL SINGHDGRYG TCHTPMKFWA AWREEDITDP
QMYALRNHPL STEQIHALFD HRPSVDLKWY QQLIDGGELA VSGQDKLLIS LLSPERLLEM
TRFFTLFDKK TGKIVARYQQ VFGIKRLLER ISTRRPDGGR EGGVIWHTTG SGKSYTMVFL
SKALILHDSL KQCRIVVVTD RVDLEGQLSG TFVSGGELAG KDDKAKAMAT SGQKLAQQIG
SGKERIIFTL IQKFNSATKL PECVNTSPDI IVLIDEGHRS QGGENHVRMK LALPNAAFVA
FTGTPLLKED KTTNKFGPIV HAYTMQRAVE DKAVTPLLYE ERIPDLEVND RAIDAWFDRI
TDGLSEAQKA DLKRKYARKG EVYSADDRIR LIALDIATHF SKNIDEGLKG QLACDSKISA
IKYKKYLDEA GLFESAVVIS PPDTREGNTE VDESKLPEVT KWWKDNVGTQ DESVYTRNII
SRFDTDEKLK LLIVVDKLLT GFDEPKNTVL YIDKPLKSHN LIQAIARVNR LHPLKKFGLL
IDYRGILAEL DTTIGKYQDL ASRTQGGYDI KDIDGLYSAM SSEYKRLPHL YNQLWAIFAG
VKNKNDTEQL RAVLVPKMEE RDGEMVDIHQ KTRDDFFEAL TAFAGCLKVA LQSATFFTDK
SFTEQDRNLY KETVKQMSSL RQWAMQVSGE QVNYDDYAEQ VKKLLDKHVT GVEVREPDGV
YEVGKMGKSE KPEEWDNNKT RNETDIIKTR VTKMIEQELR DDPYAQEAFS KLLRMAIEEA
EKLFDHPLKQ YLLFREFEEQ VEARKLSDIP DALAVNKHAQ AYYGVFKKEL PEVFAVNDVQ
VQDKWTKLAF EVDNIIVKAV AENSLNPQDI EKVVKTSLLP LLFTACREIG AGMNQVNRIV
ETIIQILRVG LMKS
//
