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Replication initiator protein (Rep75 protein) (EC 2.7.7.31) (EC 3.1.21.-) (EC 6.5.1.1) (ORF1)

 REP75_PYRAB             Reviewed;         654 AA.
O54003;
28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
12-SEP-2018, entry version 41.
RecName: Full=Replication initiator protein;
Short=Rep75 protein;
EC=2.7.7.31;
EC=3.1.21.-;
EC=6.5.1.1;
AltName: Full=ORF1;
Name=rep75; Synonyms=orf1;
Pyrococcus abyssi (strain GE5 / Orsay).
Plasmid pGT5.
Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
Pyrococcus.
NCBI_TaxID=272844;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, COFACTOR,
BIOPHYSICOCHEMICAL PROPERTIES, AND DNA-BINDING.
STRAIN=GE5 / Orsay;
PubMed=9570403; DOI=10.1046/j.1365-2958.1998.00759.x;
Marsin S., Forterre P.;
"A rolling circle replication initiator protein with a nucleotidyl-
transferase activity encoded by the plasmid pGT5 from the
hyperthermophilic archaeon Pyrococcus abyssi.";
Mol. Microbiol. 27:1183-1192(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=GE5 / Orsay;
PubMed=8655503; DOI=10.1128/jb.178.11.3232-3237.1996;
Erauso G., Marsin S., Benbouzid-Rollet N., Baucher M.F., Barbeyron T.,
Zivanovic Y., Prieur D., Forterre P.;
"Sequence of plasmid pGT5 from the archaeon Pyrococcus abyssi:
evidence for rolling-circle replication in a hyperthermophile.";
J. Bacteriol. 178:3232-3237(1996).
[3]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, DNA
SEQUENCE-SPECIFICITY, AND MUTAGENESIS OF TYR-448 AND ARG-451.
STRAIN=GE5 / Orsay;
PubMed=10417644; DOI=10.1046/j.1365-2958.1999.01498.x;
Marsin S., Forterre P.;
"The active site of the rolling circle replication protein Rep75 is
involved in site-specific nuclease, ligase and nucleotidyl transferase
activities.";
Mol. Microbiol. 33:537-545(1999).
[4]
FUNCTION AS A TOPOISOMERASE, AND MUTAGENESIS OF TYR-448 AND ARG-451.
STRAIN=GE5 / Orsay;
PubMed=10871346; DOI=10.1093/nar/28.11.2251;
Marsin S., Marguet E., Forterre P.;
"Topoisomerase activity of the hyperthermophilic replication initiator
protein Rep75.";
Nucleic Acids Res. 28:2251-2255(2000).
-!- FUNCTION: Required for rolling circle plasmid replication, has a
site-specific endonuclease/ligase activity (nicking and closing).
In vitro (no in vivo system yet exists) cleaves the double-
stranded origin of replication (dso) site, on an ssDNA template,
remaining covalently linked to the 5' end. Religates the
appropriate substrates. Has nucleotidyltransferase activity,
adding ATP or dATP to the 3' end of the nicked ssDNA site. Both
activities require a G nucleotide at the 3' end of the nicking
site. Also has topoisomerase activity, nicking and relaxing
negatively supercoiled plasmids in a narrow concentration range
(25-50 molar ratio of protein:DNA). Topoisomerase is not dependent
on a dso sequence. Has no topoisomerase activity on slightly
positively supercoiled plasmid. {ECO:0000269|PubMed:10417644,
ECO:0000269|PubMed:10871346, ECO:0000269|PubMed:9570403}.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1).
-!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
AMP + diphosphate.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:9570403};
Note=DNA nicking and nucleotidyltransferase are strictly dependent
on Mn(2+); Mg(2+) is able to substitute in DNA nicking 5X less
efficiently. {ECO:0000269|PubMed:9570403};
-!- ACTIVITY REGULATION: ATP and dATP inhibit nicking and closing
while stimulating nucleotidyltransferase.
{ECO:0000269|PubMed:10417644}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Temperature dependence:
Optimum temperature is 105 degrees Celsius for ssDNA nicking, 75
degrees Celsius for nucleotidyltransferase activity on a ssDNA
substrate. Optimum temperature for ssDNA closing is substrate
dependent, being 55 and 75 degrees Celsius for the 2 substrates
tested. Topoisomerase activity is only seen between 55 and 75
degrees Celsius. {ECO:0000269|PubMed:10417644,
ECO:0000269|PubMed:9570403};
-!- PTM: The N-terminus is blocked when overexpressed in E.coli.
-!- MISCELLANEOUS: Plasmids from hyperthermophilic archaea are relaxed
to positively supercoiled at physiological temperatures.
-!- SIMILARITY: Belongs to the Gram-positive plasmids replication
protein type 1 family. {ECO:0000305}.
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EMBL; AJ002587; CAA05626.1; -; Genomic_DNA.
EMBL; U49503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
SMR; O54003; -.
OrthoDB; POG093Z02MW; -.
BRENDA; 2.7.7.31; 5242.
Proteomes; UP000000810; Plasmid pGT5.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
GO; GO:0003912; F:DNA nucleotidylexotransferase activity; IEA:UniProtKB-EC.
GO; GO:0003916; F:DNA topoisomerase activity; IEA:UniProtKB-KW.
GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0006276; P:plasmid maintenance; IEA:UniProtKB-KW.
1: Evidence at protein level;
ATP-binding; Coiled coil; Complete proteome; DNA replication;
DNA-binding; Endonuclease; Hydrolase; Isomerase; Ligase; Nuclease;
Nucleotide-binding; Plasmid; Plasmid copy control; Topoisomerase;
Transferase.
CHAIN 1 654 Replication initiator protein.
/FTId=PRO_0000420230.
COILED 535 585 {ECO:0000255}.
ACT_SITE 448 448 O-(5'-phospho-DNA)-tyrosine intermediate.
{ECO:0000305}.
MUTAGEN 448 448 Y->F: Loss of nicking and closing
activities, binds, not covalently, to
ssDNA. Still has nucleotidyltransferase
activity. Loss of topoisomerase activity.
Loss of all activities; when associated
with L-451. {ECO:0000269|PubMed:10417644,
ECO:0000269|PubMed:10871346}.
MUTAGEN 451 451 R->L: Loss of nucleotidyltransferase
activity, reduced DNA closing but no loss
of ssDNA nicking. Decreased plasmid
nicking, no closing activity on
supercoiled plasmids. Loss of all
activities; when associated with F-448.
{ECO:0000269|PubMed:10417644,
ECO:0000269|PubMed:10871346}.
SEQUENCE 654 AA; 75224 MW; 16635E4BBDA50BB4 CRC64;
MVIYTSKFKN SLLDGLGVGH LSYDDQPILC NEVHPTLTLD TFISGGSSGS RPRPRWVYLD
ISTTNEGISE EFSSNTESKS PLLKVCGVSS KSSEGDGSSF IWFDKYRSVI SRLEHSGFVE
VERTVLKLRK ISKELRSINK QLSRLFLDDR ERAKLLSRKR KYLDFARALI GSISKSLTLY
ADRFFVEVPQ DYAKLIQKLG FSSDTLLLHL FVNSGVLEVF LDDNSSHKFR IAYISKVHAG
KYHPVKGISK GSQEAKRVLR DLLVLSELLE GSLVSYRSGG VETIHHLIPV RHFVLTAPKE
LSFSIWASLK KGDSSLFRAF KDAGAKAIKE FLSYLASKEH ISGNLLFGFT INVHVTGDKN
PFEPHFHIDA IVTFICYDKS STKWFRLNPL LSESDLKKLR DIWKNVLLSY FGELLSEDTK
SKDFDVWAGD NYYSLPLDVP QVFFELKYAS RKLFVNFVNY FEQSNFDESS VSDWDFVRFV
FEYSNRTERY GFLTNIKRYL SMSCSHLVEK RVQELEEFIS RIEFDLSVNG NKMSDSLKRA
LLERLEYLKD ELSELKERGF EYLFERALEK AEELLSNDNL TLERVIHILE TLFTALGKSI
VNYNFYVELE DVSFREFVDY LYDNHLSDVL VFSDRHRSIT IIRLIPPPDG GVPV


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