ID   DPO3_STRPB              Reviewed;        1465 AA.
AC   Q1J9R4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
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};
GN   OrderedLocusNames=MGAS2096_Spy1695;
OS   Streptococcus pyogenes serotype M12 (strain MGAS2096).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=370553;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS2096;
RX   PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA   Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA   Musser J.M.;
RT   "Molecular genetic anatomy of inter- and intraserotype variation in the
RT   human bacterial pathogen group A Streptococcus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
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; CP000261; ABF36747.1; -; Genomic_DNA.
DR   RefSeq; WP_002988040.1; NC_008023.1.
DR   AlphaFoldDB; Q1J9R4; -.
DR   SMR; Q1J9R4; -.
DR   KEGG; spj:MGAS2096_Spy1695; -.
DR   HOGENOM; CLU_003297_2_0_9; -.
DR   OMA; YYAAYFT; -.
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; 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; IPR016195; Pol/histidinol_Pase-like.
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; 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   SUPFAM; SSF89550; SSF89550; 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; Transferase.
FT   CHAIN           1..1465
FT                   /note="DNA polymerase III PolC-type"
FT                   /id="PRO_1000048484"
FT   DOMAIN          427..583
FT                   /note="Exonuclease"
SQ   SEQUENCE   1465 AA;  164640 MW;  679F5A68CBB63B3E CRC64;
     MSDLFAKLMD QIEMPLDMRR SSAFSSADII EVKVHSVSRL WEFHFAFAAV LPIATYRELH
     DRLIRTFEAA DIKVTFDIQA AQVDYSDDLL QAYYQEAFEH APCNSASFKS SFSKLKVTYE
     DDKLIIAAPG FVNNDHFRNN HLPNLVKQLE AFGFGTLTID MVSDQEMTEH LTKDFVSSRQ
     ALVKKAVQDN LEAQKSLEAM MPPVEEATPA PKFDYKERAA KRQAGFEKAT ITPMIEIETE
     ENRIVFEGMV FDVERKTTRT GRHIINFKMT DYTSSFALQK WAKDDEELRK FDMIAKGAWL
     RVQGNIETNP FTKSLTMNVQ QVKEIVHHDR KDLMPEGQKR VELHAHTNMS TMDALPTVES
     LIDTAAKWGH KAVAITDHAN VQSFPHGYHR ARKAGIKAIF GLEANIVEDK VPISYDPVDM
     DLHEATYVVF DVETTGLSAM NNDLIQIAAS KMFKGNIVEQ FDEFIDPGHP LSAFTTELTG
     ITDKHLQGAK PLVTVLKAFQ DFCKDSILVA HNASFDVGFM NANYERHDLP KITQPVIDTL
     EFARNLYPEY KRHGLGPLTK RFQVSLDHHH MANYDAEATG RLLFIFLRDA REKHGIKNLL
     QLNTDLVAED SYKKARIKHA TIYVQNQVGL KNMFKLVSLS NIKYFEGVPR IPRTVLDAHR
     EGLLLGTACS DGEVFDAVLT KGIDAAVDLA KYYDFIEIMP PAIYQPLVVR ELIKDQAGIE
     QVIRDLIEVG KRAKKPVLAT GNVHYLEPEE EIYREIIVRS LGQGAMINRT IGRGEGAQPA
     PLPKAHFRTT NEMLDEFAFL GKDLAYQVVV QNTQDFADRI EEVEVVKGDL YTPYIDKAEE
     TVAELTYQKA FEIYGNPLPD IIDLRIEKEL TSILGNGFAV IYLASQMLVN RSNERGYLVG
     SRGSVGSSFV ATMIGITEVN PMPPHYVCPS CQHSEFITDG SVGSGYDLPN KPCPKCGTPY
     QKDGQDIPFE TFLGFDGDKV PDIDLNFSGD DQPSAHLDVR DIFGDEYAFR AGTVGTVAEK
     TAYGFVKGYE RDYGKFYRDA EVDRLAAGAA GVKRTTGQHP GGIVVIPNYM DVYDFTPVQY
     PADDVTASWQ TTHFNFHDID ENVLKLDILG HDDPTMIRKL QDLSGIDPIT IPADDPGVMA
     LFSGTEILGV TPEQIGTPTG MLGIPEFGTN FVRGMVNETH PTTFAELLQL SGLSHGTDVW
     LGNAQDLIKE GIATLKTVIG CRDDIMVYLM HAGLEPKMAF TIMERVRKGL WLKISEEERN
     GYIDAMRENN VPDWYIESCG KIKYMFPKAH AAAYVLMALR VAYFKVHHPI MYYCAYFSIR
     AKAFELKTMS GGLDAVKARM EDITIKRKNN EATNVENDLF TTLEIVNEML ERGFKFGKLD
     LYKSDAIEFQ IKGDTLIPPF IALEGLGENV AKQIVKARQE GEFLSKMELR KRGGASSTLV
     EKMDEMSILG NMPEDNQLSL FDDFF