DPO3_STRMU
ID DPO3_STRMU Reviewed; 1465 AA.
AC Q8DWE0;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=DNA polymerase III PolC-type {ECO:0000255|HAMAP-Rule:MF_00356};
DE Short=PolIII {ECO:0000255|HAMAP-Rule:MF_00356};
DE EC=2.7.7.7 {ECO:0000255|HAMAP-Rule:MF_00356};
GN Name=polC {ECO:0000255|HAMAP-Rule:MF_00356}; OrderedLocusNames=SMU_123;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC -!- FUNCTION: Required for replicative DNA synthesis. This DNA polymerase
CC also exhibits 3' to 5' exonuclease activity. {ECO:0000255|HAMAP-
CC Rule:MF_00356}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00356};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00356}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. PolC
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00356}.
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DR EMBL; AE014133; AAN57903.1; -; Genomic_DNA.
DR RefSeq; NP_720597.1; NC_004350.2.
DR RefSeq; WP_002263483.1; NC_004350.2.
DR AlphaFoldDB; Q8DWE0; -.
DR SMR; Q8DWE0; -.
DR STRING; 210007.SMU_123; -.
DR PRIDE; Q8DWE0; -.
DR EnsemblBacteria; AAN57903; AAN57903; SMU_123.
DR KEGG; smu:SMU_123; -.
DR PATRIC; fig|210007.7.peg.104; -.
DR eggNOG; COG2176; Bacteria.
DR HOGENOM; CLU_003297_2_0_9; -.
DR OMA; YYAAYFT; -.
DR PhylomeDB; Q8DWE0; -.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.150.700; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR HAMAP; MF_00356; DNApol_PolC; 1.
DR InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR InterPro; IPR040982; DNA_pol3_finger.
DR InterPro; IPR024754; DNA_PolC-like_N_II.
DR InterPro; IPR028112; DNA_PolC-type_N_I.
DR InterPro; IPR029460; DNAPol_HHH.
DR InterPro; IPR006054; DnaQ.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR006308; PolC_gram_pos.
DR InterPro; IPR044923; PolC_middle_finger_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF14480; DNA_pol3_a_NI; 1.
DR Pfam; PF11490; DNA_pol3_a_NII; 1.
DR Pfam; PF07733; DNA_pol3_alpha; 2.
DR Pfam; PF17657; DNA_pol3_finger; 1.
DR Pfam; PF14579; HHH_6; 1.
DR Pfam; PF02811; PHP; 1.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00479; EXOIII; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR TIGRFAMs; TIGR00573; dnaq; 1.
DR TIGRFAMs; TIGR01405; polC_Gram_pos; 1.
PE 3: Inferred from homology;
KW Cytoplasm; DNA replication; DNA-directed DNA polymerase; Exonuclease;
KW Hydrolase; Nuclease; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..1465
FT /note="DNA polymerase III PolC-type"
FT /id="PRO_0000204597"
FT DOMAIN 425..581
FT /note="Exonuclease"
SQ SEQUENCE 1465 AA; 165568 MW; 9234EB15BAF5C4B3 CRC64;
MSELFKKLMD QIEMPLEMKN SRVFSSADIV EVKVYPESRI WDFRFSFETI LPIDFYQELR
SRLVTSFETA DIKAVFDIEV ENAEFSNELL QAYYQEAFKQ PTCNSASFKS SFSHLTVSYT
DGKVLISAPQ FVNNDHFRKN HLPNLEKQFE AFGFGKLSFD IVSNQKMTEE IKHHFESSRQ
QQIQKASQET LEIQKSLEAS IPPEEIPKPV SNFKERIKDR QAAFEKAEIT PMAEIETEEN
RITFEGLVFD VERKTTRTGR HIINFKMTDY TSSFPMQKWA KDDEELKKYD MISKGAWLRV
RGNIENNPFT KALTMNVQNV KTIVHKERKD LMPQGEKRVE FHAHTNMSTM DALPTVEQLV
AKAAQFGHPA VAITDHGNVQ SFPHGYHAGK KNGIKVLFGL EANLVEDRVP IVYNEVDMDM
NEATYVVFDV ETTGLSAINN DLIQIAASKM HKGNIVEQFD EFIDPGHPLS QFTTDLTGIT
DQHVKGAKPI SQVLQEFQSF CQDTVLVAHN ATFDVGFMNA NYERHDLPKI TQPVIDTLEF
ARNLYPEYKR HGLGPLTKRF QVSLEHHHMA NYDAEATGRL LFIFLKEAKE KHGVNNLLDL
NTKIVDDNSY KKARVKHATI YVLNQKGLKN LFKLVSLSNV TYFAGVARIP RTILDQYRDG
LLLGTACSDG EVFDTVLSKG VEDAVEVAKY YDFIEVMPPA LYEPLLAREL IKDEAGIQQI
IKDLIEVGRR LDKPVLATGD VHYLEPEDEI YREIIVRSLG QGAMINRPIG RGENAQPAPL
PKAHFRTTNE MLDEFAFLGE DLARDIVIKN PNEMVERFED VEVVKTDLYT PFIENSEEKV
AEMTYEKAFE IYGNPLPDII DLRIEKELTS ILGNGFAVIY LASQMLVNRS NERGYLVGSR
GSVGSSFVAT MIGITEVNPM PPHYICPNPD CKHSEFITDG SVGSGYDLPD KICSECGTPY
KKDGQDIPFE TFLGFDGDKV PDIDLNFSGD DQPSAHLDVR DIFGEEYAFR AGTVGTVADR
TAYGFVKGYE RDYGKFYRDA EVDRLAQGSA GVKRTTGQHP GGIVVIPNYM DVYDFTPVQY
PADDLTAEWQ TTHFNFHDID ENVLKLDVLG HDDPTMIRKL QDLSGIDPKT IPADDPEVMK
LFSGTEVLGV TEEEIGTPTG MLGIPEFGTN FVRGMVDETH PTTFAELLQL SGLSHGTDVW
LGNAQDLIKQ GIATLSTVIG CRDDIMVYLM HAGLEPKMAF TIMERVRKGA WLKISEEERN
GYISAMRENN VPDWYIESCG KIKYMFPKAH AAAYVLMALR VAYFKVHHPI YYYCAYFSIR
AKAFELKTMS AGLDAVKARM ADISQKRKIN QASNVEIDLF TTLEIVNEML ERGFKFGQLD
LYRSDATEFI IDGDTLIPPF VALEGLGENV AKQIVKARNE GEFLSKTELR KRGGLSSTLV
EKMSDMGILG SMPEDNQLSL FDDFF
