ID   DPOL2_METTH             Reviewed;         223 AA.
AC   O26310;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=DNA polymerase PolB subunit 2;
DE            EC=2.7.7.7;
GN   Name=polB2; OrderedLocusNames=MTH_208;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
RN   [2]
RP   FUNCTION AS A DNA POLYMERASE, FUNCTION AS AN EXONUCLEASE, CATALYTIC
RP   ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION
RP   WITH POLB1, AND SUBUNIT.
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=10497247; DOI=10.1074/jbc.274.40.28751;
RA   Kelman Z., Pietrokovski S., Hurwitz J.;
RT   "Isolation and characterization of a split B-type DNA polymerase from the
RT   archaeon Methanobacterium thermoautotrophicum deltaH.";
RL   J. Biol. Chem. 274:28751-28761(1999).
CC   -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC       exhibits 3'-5' exonuclease activity. {ECO:0000269|PubMed:10497247}.
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:10497247};
CC   -!- ACTIVITY REGULATION: DNA polymerase is inhibited by replication protein
CC       A (RPA), while 3'-5' exonuclease activity is not. Polymerase inhibition
CC       can be overcome by replication factor C (RFC) and PCNA.
CC       {ECO:0000269|PubMed:10497247}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Optimum temperature for DNA polymerase is 60 degrees Celsius,
CC         functional between 60 and 80 degrees Celsius. Exonuclease activity is
CC         higher at 70 than 50 degrees Celsius. {ECO:0000269|PubMed:10497247};
CC   -!- SUBUNIT: Formed of a complex between PolB1 and PolB2; the exonuclease
CC       activity is associated with subunit 1. Probably binds replication
CC       protein A (RPA). {ECO:0000269|PubMed:10497247}.
CC   -!- MISCELLANEOUS: In some Methanobacteriaceae the PolB protein is split
CC       over 2 genes.
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DR   EMBL; AE000666; AAB84714.1; -; Genomic_DNA.
DR   PIR; E69125; E69125.
DR   RefSeq; WP_010875847.1; NC_000916.1.
DR   AlphaFoldDB; O26310; -.
DR   SMR; O26310; -.
DR   STRING; 187420.MTH_208; -.
DR   EnsemblBacteria; AAB84714; AAB84714; MTH_208.
DR   GeneID; 1470169; -.
DR   KEGG; mth:MTH_208; -.
DR   PATRIC; fig|187420.15.peg.177; -.
DR   HOGENOM; CLU_1173378_0_0_2; -.
DR   OMA; KQIGPHV; -.
DR   Proteomes; UP000005223; Chromosome.
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:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.132.60; -; 1.
DR   Gene3D; 3.90.1600.10; -; 1.
DR   InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR042087; DNA_pol_B_thumb.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
PE   1: Evidence at protein level;
KW   DNA replication; DNA-binding; DNA-directed DNA polymerase; Exonuclease;
KW   Hydrolase; Nuclease; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..223
FT                   /note="DNA polymerase PolB subunit 2"
FT                   /id="PRO_0000429011"
SQ   SEQUENCE   223 AA;  25528 MW;  5611F48F9A1FF6DF CRC64;
     MSQLSKVEDE ILSQVKRFLK HINSNLPEGM ELEFEGFYRR GFFVTKKRYA LIEDDTIVAK
     GLELVRRDWA PIAKKTQRKV LMAILRDGSP EKAREIIREV VGRIRRGDVE LDDLVIHTQI
     TRDLSEYKQI GPHVIAAKRS LEKGRRVERG SIVRYIIVKG RGPISQRAFP VEDAEGMGYD
     PDYYIENQVM AAVSRIMSSL GYSTEDMNSL SSGERQSSLD AFF