PIPOL_ECOLX
ID PIPOL_ECOLX Reviewed; 866 AA.
AC P0DPS1;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2019, sequence version 1.
DT 25-MAY-2022, entry version 6.
DE RecName: Full=Primer-independent DNA polymerase PolB {ECO:0000303|PubMed:29117562};
DE Short=piPolB {ECO:0000303|PubMed:29117562};
DE EC=2.7.7.- {ECO:0000269|PubMed:29117562};
DE EC=3.1.11.- {ECO:0000269|PubMed:29117562};
DE AltName: Full=Primer-dependent DNA polymerase PolB {ECO:0000305};
DE EC=2.7.7.7 {ECO:0000269|PubMed:29117562};
GN Name=pi-polB; ORFNames=AB47_1109;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3-373-03_S1_C2;
RA Silbergeld E., Coles C., Seidman J.C., You Y., George J., Nadendla S.,
RA Daugherty S.C., Nagaraj S., Ott S., Klega K., Rasko D.;
RT "Genetic variability of E. coli after antibiotic treatment.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, DOMAIN, AND MUTAGENESIS OF
RP 59-ASP--GLU-61; ASP-368; LYS-613; HIS-614; LYS-623 AND ARG-625.
RC STRAIN=3-373-03_S1_C2;
RX PubMed=29117562; DOI=10.1016/j.celrep.2017.10.039;
RA Redrejo-Rodriguez M., Ordonez C.D., Berjon-Otero M., Moreno-Gonzalez J.,
RA Aparicio-Maldonado C., Forterre P., Salas M., Krupovic M.;
RT "Primer-independent DNA synthesis by a family B DNA polymerase from self-
RT replicating mobile genetic elements.";
RL Cell Rep. 21:1574-1587(2017).
CC -!- FUNCTION: DNA polymerase with primer-independent templated DNA
CC polymerization activity, primer-dependent DNA polymerization activity
CC with strand displacement, translesion synthesis activity across non-
CC bulky base damage, 3'-5' exodeoxyribonuclease activity, and de novo
CC primer synthesis activity. The enzyme is processive and faithful.
CC Translation synthesis across abasic sites is coupled to de novo primer
CC synthesis. Overexpression of wild-type protein increases survival of
CC cells upon mitomycin C or UV treatment. {ECO:0000269|PubMed:29117562}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC Evidence={ECO:0000269|PubMed:29117562};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:29117562};
CC Note=Translesion synthesis across abasic sites is more efficient with
CC Mn(2+) compared to Mg(2+), replication of undamaged template is more
CC efficient with Mg(2+). {ECO:0000269|PubMed:29117562};
CC -!- MISCELLANEOUS: Encoded in a mobile genetic element called pipolin.
CC {ECO:0000303|PubMed:29117562}.
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DR EMBL; JNMI01000006; KDT81534.1; -; Genomic_DNA.
DR AlphaFoldDB; P0DPS1; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR SUPFAM; SSF56672; SSF56672; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; DNA replication; DNA-binding;
KW DNA-directed DNA polymerase; Exonuclease; Hydrolase; Magnesium; Manganese;
KW Nuclease; Nucleotidyltransferase; Transferase.
FT CHAIN 1..866
FT /note="Primer-independent DNA polymerase PolB"
FT /id="PRO_0000446010"
FT REGION 50..286
FT /note="Exonuclease domain"
FT /evidence="ECO:0000305|PubMed:29117562"
FT REGION 287..385
FT /note="Palm1 domain"
FT /evidence="ECO:0000305|PubMed:29117562"
FT REGION 386..481
FT /note="TPR1 domain"
FT /evidence="ECO:0000305|PubMed:29117562"
FT REGION 482..522
FT /note="Fingers domain"
FT /evidence="ECO:0000305|PubMed:29117562"
FT REGION 523..549
FT /note="TPR2 domain"
FT /evidence="ECO:0000305|PubMed:29117562"
FT REGION 550..678
FT /note="Palm2 domain"
FT /evidence="ECO:0000305|PubMed:29117562"
FT REGION 679..866
FT /note="Thumb domain"
FT /evidence="ECO:0000305|PubMed:29117562"
FT MUTAGEN 59..61
FT /note="DTE->ATA: Decreased 3'-5' exonuclease activity."
FT /evidence="ECO:0000269|PubMed:29117562"
FT MUTAGEN 368
FT /note="D->A: No primer-dependent or primer-independent DNA
FT polymerization, loss of translesion DNA synthesis."
FT /evidence="ECO:0000269|PubMed:29117562"
FT MUTAGEN 613
FT /note="K->A: Strongly reduced primer synthesis, loss of
FT translesion DNA synthesis, normal polymerase activity."
FT /evidence="ECO:0000269|PubMed:29117562"
FT MUTAGEN 614
FT /note="H->A: Normal primer synthesis and polymerase
FT activity."
FT /evidence="ECO:0000269|PubMed:29117562"
FT MUTAGEN 623
FT /note="K->A: No primer synthesis, impaired polymerase
FT activity."
FT /evidence="ECO:0000269|PubMed:29117562"
FT MUTAGEN 625
FT /note="R->A: No primer synthesis, impaired polymerase
FT activity."
FT /evidence="ECO:0000269|PubMed:29117562"
SQ SEQUENCE 866 AA; 97845 MW; D83C516B18A3A7B3 CRC64;
MSNNLQDILA AASGYQSVTS EPALNRKRPK TLDDYPVIPP ASKKVSVISS DLTLHIGFDT
EYVFNPETRQ NDILSYQSYV VLPDNTGISN IIYPPDSQKK SRLSFKDFLC QTITPLLETG
VITKWPGIIN IYAHFIRADI ASFANFWSDY KILLKGIRGT VSSFKNRYGI DFDEQQERRV
KTEQIMFDKR TSPPRCSNVA FIDTLLITPG GMGLAECGEL LGLPKLTIPA PYSITNMREY
LLGDRAGFEA YALRDAEIAV RYALQVRNFC ARELMIDRVP ATIGAMAVSR FTKTLKENNM
SPEVCLGTHI KTRELWLTEK QAFRTIKNPA SVPSRELFET FPINCYHGGR NECFMMGVTP
SDHWYDYDLA GAYTTGLLDI LTPDYGNIRL SKNPDDYCGH VMGFALVTFR FPESVPYPSL
PVRTDQYGLF FPLSGESWAT APEIELALSL GAEMTIHNGI IVPWICDTSP HNSESTSVFL
PFVQQVRENR NRHIKGSLEE KFWKEIGNSL YGKLAQGLRA KTAFDTARGL NRSLPPSSVT
QPFFAAHVTG FIRAVVGELM NALPSDSSVV SVTTDGFLTN CPLDKINMSG PLSSRFQSLC
DIVDPGSSML TCKHEVSQLI AMKTRGQLTY KAIQGKPVVH ARAGVKPPAD IPRSDYNDYM
VDLYLNRLPG QTLSRSTLIS TREMWLSESD LVSREQDIRL NLEFDFKRQP VRPAMNEGHL
LMFSRPWDNM EEALQQRSLF DDWRQTHTLK TLADWDDWCD FLYCRTVFSD MKLKVGSKRS
DDILVRLFLR ALTQCQWGLM LKDKKSYSCK EVAEWLTSEG YSVTVTDVKN AVRAKIPQMK
FSSVTPRMKS LMDIIARKYP TFCLPV
