DPO3_STRT1
ID DPO3_STRT1 Reviewed; 1464 AA.
AC Q5M1Y0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=str0062;
OS Streptococcus thermophilus (strain CNRZ 1066).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=299768;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNRZ 1066;
RX PubMed=15543133; DOI=10.1038/nbt1034;
RA Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT "Complete sequence and comparative genome analysis of the dairy bacterium
RT Streptococcus thermophilus.";
RL Nat. Biotechnol. 22:1554-1558(2004).
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; CP000024; AAV61679.1; -; Genomic_DNA.
DR RefSeq; WP_011226747.1; NC_006449.1.
DR AlphaFoldDB; Q5M1Y0; -.
DR SMR; Q5M1Y0; -.
DR GeneID; 66897995; -.
DR KEGG; stc:str0062; -.
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; 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; 1.
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; Transferase.
FT CHAIN 1..1464
FT /note="DNA polymerase III PolC-type"
FT /id="PRO_1000048493"
FT DOMAIN 426..582
FT /note="Exonuclease"
SQ SEQUENCE 1464 AA; 164844 MW; 12D7492F17F0B05A CRC64;
MSDKFKLLLK QIHFPQHEEA YNEIKSGSIE SVKLFKSKRQ WFFVFSFRNL LSYETFTLFD
NLLHSSFDSL GAKVSYMINV EDISCDQSLL EAYFSYALDI LKSSHFSIYS LFSNLGIEIS
NNSISVKAPA HILRENLHER FIALIADVLS NVGLSNVSIS VLEDKEASSS LEEAYETNKI
SLQEEAESQA RQALQSIVQS SPVPPPQKHQ AQNFAEKQSQ RVASFDKAEI TPMIEVNSEE
NRIVFEGYIF DVEQRETKTG RIIINFKVTD YTSSFAMQRW VKDSEELVKF GMIKKGNWVR
VRGRIENNPF THSLTMNVQD IKEISHTPRK DLMPEGQKRV EFHAHTNMST MDAIPTVEEL
IDTAAFWGHP AVAITDHANV QSFPHGYHKA KKAGIKAIFG LEANLVEDKV PIVYNSENLE
LKEATYVVFD VETTGLSAVH NDLIQIAASK MHKGNIVEQF DEFIDPGYPL SAFTTELTGI
TDNHVKGAKP LVQVLQEFQE FCKGAVLVAH NATFDVGFMN ANYERHQLPT ISQPVIDTLE
FARNLYPEYK RHGLGPLTKR FGVALDHHHM ANYDAEATGR LLFIFIKDVF EKHGLTNLEQ
LNTELVSDDS YKKSRVKHAT LYVQNQTGLK NIFKLVSLSN VSYFEGVARI PRKVLDEYRE
GIIVGSACAD GEVFDTLLSH GIDKAVEVAK YYDFIEVMPP AIYAPLIAKD LIKDEGAIEQ
LIRDLIEVAN RLDKPVLATG NVHYINPEDA IYREIIVRAL GQGAMINRPI GKEENAQPAP
LPEAHFRTTN EMLDEFAFLG KDLAYEIVVA NTQAMANQIE EVEVVKKDLY TPYIDRAEEQ
VAEMTYAKAF ELYGNPLPDI IDLRIEKELS SILGNGFAVI YLASQMLVNR SNERGYLVGS
RGSVGSSFVA TMIGITEVNP MPPHYLCPKC QHSEFITDGS YGSGFDLPDK ECSECGTEYK
KDGQDIPFET FLGFDGDKVP DIDLNFSGDD QPSAHLDVRD IFGEQYAFRA GTVGTVADRT
AYGFVKGYER DYNKFYRDAE VDRLAMGVAG VKRNTGQHPG GIVVIPNYMD VYDFTPVQYP
ADDVTAAWQT THFNFHDIDE NVLKLDILGH DDPTMIRKLQ DLSGIDPKDI RADDPDVMKL
FSGTEVLGVT PEQIGTSTGV LGIPEFGTNF VRGMVEETHP TTFAELLQLS GLSHGTDVWL
GNAQDLIKEG IATLKTVIGC RDDIMVYLMH AGLDPKMAFT IMERVRKGMW LKISEEERNG
YIQAMRENNV PDWYIESCGK IKYMFPKAHA AAYVMMALRV AYFKVHHPIY YYCAYFSIRA
KAFELKTMSA GLDAVKARME DIKEKRQRNE ATNLENDLFT TLEIVNEMLE RGFTFGQLDL
YKSQATEFLI EGDTLIPPFI ALEGLGENVA KQLVAAREEG EFLSKTELRK RGGLSSTLVE
RLDEMGILGN MPEDNQLSLF DDFF
