DPO3_STRSV
ID DPO3_STRSV Reviewed; 1462 AA.
AC A3CQI2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=SSA_2066;
OS Streptococcus sanguinis (strain SK36).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=388919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK36;
RX PubMed=17277061; DOI=10.1128/jb.01808-06;
RA Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL J. Bacteriol. 189:3166-3175(2007).
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; CP000387; ABN45437.1; -; Genomic_DNA.
DR RefSeq; WP_011837528.1; NC_009009.1.
DR RefSeq; YP_001035987.1; NC_009009.1.
DR AlphaFoldDB; A3CQI2; -.
DR SMR; A3CQI2; -.
DR STRING; 388919.SSA_2066; -.
DR EnsemblBacteria; ABN45437; ABN45437; SSA_2066.
DR KEGG; ssa:SSA_2066; -.
DR PATRIC; fig|388919.9.peg.1959; -.
DR eggNOG; COG2176; Bacteria.
DR HOGENOM; CLU_003297_2_0_9; -.
DR OMA; YYAAYFT; -.
DR OrthoDB; 561611at2; -.
DR Proteomes; UP000002148; 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; Reference proteome;
KW Transferase.
FT CHAIN 1..1462
FT /note="DNA polymerase III PolC-type"
FT /id="PRO_1000048491"
FT DOMAIN 424..580
FT /note="Exonuclease"
SQ SEQUENCE 1462 AA; 164738 MW; CC5366F96C90498E CRC64;
MSNKFEILMN QLDMPLEMRN SEAFLNAEIE KVLVHKVSRV WEFHFSFANI LPIEIFRELQ
KRLAQEFSKT GNQAVFEIHC QAPQVSDELL QAYYQLAFEE GPCASHGFKS LYQDLRVHLD
GDKLLIEGAS TIDTEHFRKN HLPNLSQQLV KYGFPQLTCL VQHSDELTQQ QAENFQAEND
KIVQAANEEA LKAMESLQQM APPPEEKPAY DFQARKAAAK PKLDKAEITP MIEVQTEENR
LVFEGMVFDL EQKVTRTGRV LLNFKMTDYT SSFSLQKWMK NEEEAKKFDM IKKGAWLRVR
GNVEMNNFTR DLTMNVQDVQ AVTHYERKDL MPEGQKRVEF HAHTNMSTMD ALPEVEEIVA
TAAKWGHKAV AITDHGNVQS FPHGYKAAKK AGIQLIYGME ANIVEDRVPI VYNEVDMELS
DATYVVFDVE TTGLSAVYND LIQVAASKMH KGNIIAEFDE FINPGHPLSA FTTDLTGITD
EHVRNAKPLE QVLKEFQEFC QDSVLVAHNA TFDVGFMNVN YERHGLPKII QPVIDTLEFA
RNLYPEYKRH GLGPLTKRFQ IALEHHHMAN YDAEATGRLL FIFIKDVAEK HGVTNLKDLN
TDLVDENSYK KARVKHATIY VKNQTGLKNI FKLVSLSNTK YFEGVPRIPR TVLDAHREGL
ILGSACSEGE VYDAVVSQGV DAAVEVAKYY DFIEVMPPAI YEPLIAKEQI KDQEELQTII
RNLIEVGDRL GKPVLATGNV HYIEPEEEIY REIIVRSLGQ GAMINRTIGH GENAQPAPLP
KAHFRTTNEM LDEFAFLGED LAKKLVITNP NQLAETFEPV EVVKGDLYTP FIDKAEETVA
ELTYQKAFEI YGNPLPDIVD LRIEKELTSI LGNGFAVIYL ASQMLVQRSN ERGYLVGSRG
SVGSSFVATM IGITEVNPLS PHYVCGKCQY SEFITDGSYG SGFDMPDKDC PECGHKLSKN
GQDIPFETFL GFDGDKVPDI DLNFSGEDQP SAHLDVRDIF GSEYAFRAGT VGTVAAKTAY
GFVKGYERDY GKFYRDAEVE RLAQGAAGVK RTTGQHPGGI VVIPNYMDVY DFTPVQYPAD
DVTAEWQTTH FNFHDIDENV LKLDVLGHDD PTMIRKLQDL SGIDPNDIPM DDAGVMALFS
GTDILGVTQE QIGTPTGMLG IPEFGTNFVR GMVDETHPTT FAELLQLSGL SHGTDVWLGN
AQDLIKQGIA DLSTVIGCRD DIMVYLMHKG LDPKMAFTIM ERVRKGLWLK ISEEERNGYI
AAMKENNVPE WYIESCGKIK YMFPKAHAAA YVMMALRVAY FKVHHPIYYY CAYFSIRAKA
FDIKTMSGGL DAVKRRMSEI AEKRKNNEAS NVEIDLYTTL EIVNEMLERG FKFGKLDLYK
SHATEFLIEG DTLIPPFSAM DGLGDNVARQ VVRAREEGEF LSKTELRKRG GLSSTLVEKM
DDMGILGNMP EDNQLSLFDE FF
