DPO3_STRPF
ID DPO3_STRPF Reviewed; 1465 AA.
AC Q1J4M0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=MGAS10750_Spy1766;
OS Streptococcus pyogenes serotype M4 (strain MGAS10750).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=370554;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS10750;
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; CP000262; ABF38716.1; -; Genomic_DNA.
DR RefSeq; WP_011529023.1; NC_008024.1.
DR AlphaFoldDB; Q1J4M0; -.
DR SMR; Q1J4M0; -.
DR PRIDE; Q1J4M0; -.
DR EnsemblBacteria; ABF38716; ABF38716; MGAS10750_Spy1766.
DR KEGG; spi:MGAS10750_Spy1766; -.
DR HOGENOM; CLU_003297_2_0_9; -.
DR OMA; YYAAYFT; -.
DR Proteomes; UP000002434; 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; 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_1000048487"
FT DOMAIN 427..583
FT /note="Exonuclease"
SQ SEQUENCE 1465 AA; 164575 MW; 2F7949920BDE122C CRC64;
MSDLFAKLMD QIEMPLDMRR SSAFSSADII EVKVHSVSRL WEFHFAFAAV LPIATYRELH
DRLIRTFEAA DIKVTFDIQA AQVDYSDDLL QAYYQEAFEH APCNSASFKS SFSKLKVTYE
DDKLIIAAPG FVNNDHFRNN HLPNLVKQFE AFGFGTLTID MVSDQEMTEH LTKDFVSSRQ
ALVKKAVQDN LEAQKSLEAM MPPVEEATPA PKFDYKERAA KRQAGFEKAT ITPMIEIETE
ENRIVFEGMV FDVERKTTRT GRHIINFKMT DYTSSFALQK WAKDDEELRK FDMIAKGAWL
RVQGNIETNP FTKSLTMNVQ QVKEIVHHER 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 RLLFIFLKDA REKHGIKNLL
QLNTDLVAED SYKKARIKHA TIYVQNQVGL KNMFKLVSLS NIKYFEGVPR IPRTVLDAHR
EGLLLGTACS DGEVFDAVLT KGIDAAVDLA KYYDFIEIMP PAIYQPLVVR ELIKDQAGIE
QVIRDLIEVG KRANKLVLAT GNVHYLEPEE EIYREIIVRS LGQGAMINRT IGRGEGAQPA
PLPKAHFRTT NEMLDEFAFL GKDLAYQVVV ENTQDFADRI EEVEVVKGDL YTPYIDKAEE
TVAELTYQKA FEIYGNPLPD IIDLRIEKEL TSILGNGFAV IYLASQMLVN RSNERGYLVG
SRGSVGSSFV ATMIGITEVN PMPPHYVCPS CQHSEFITDG SVGSGYDLPN KPCPKCGTPY
QKDGQDIPFE TFLGFDGDKV PDIDLNFSGD DQPSAHLDVR DIFGAEYAFR AGTVGTVAEK
TAYGFVKGYE RDYGKFYRDA EVDRLAAGAA GVKRTTGQHP GGIVVIPNYM DVYDFTPVQY
PADDVTASWQ TTHFNFHDID ENVLKLDILG HDDPTMIRKL QDLSGIDPIT IPADDPGVMA
LFSGTEVLGV 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
EKMDEMGILG NMPEDNQLSL FDDFF
