DPO3_STRP2
ID DPO3_STRP2 Reviewed; 1463 AA.
AC Q04MH6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=SPD_0254;
OS Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=373153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D39 / NCTC 7466;
RX PubMed=17041037; DOI=10.1128/jb.01148-06;
RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT pneumoniae and comparison with that of unencapsulated laboratory strain
RT R6.";
RL J. Bacteriol. 189:38-51(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; CP000410; ABJ54142.1; -; Genomic_DNA.
DR RefSeq; WP_000071396.1; NC_008533.2.
DR AlphaFoldDB; Q04MH6; -.
DR SMR; Q04MH6; -.
DR STRING; 373153.SPD_0254; -.
DR EnsemblBacteria; ABJ54142; ABJ54142; SPD_0254.
DR GeneID; 60232999; -.
DR KEGG; spd:SPD_0254; -.
DR eggNOG; COG2176; Bacteria.
DR HOGENOM; CLU_003297_2_0_9; -.
DR OMA; YYAAYFT; -.
DR OrthoDB; 561611at2; -.
DR BioCyc; SPNE373153:G1G6V-279-MON; -.
DR Proteomes; UP000001452; 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..1463
FT /note="DNA polymerase III PolC-type"
FT /id="PRO_1000048483"
FT DOMAIN 425..581
FT /note="Exonuclease"
SQ SEQUENCE 1463 AA; 164776 MW; D46ACD88755AF679 CRC64;
MSNSFEILMN QLGMPAEMRQ APALAQANIE RVVVHKISKV WEFHFVFSNI LPIEIFLELK
KGLSEEFSKT GNKAVFEIKA RSQEFSNQLL QSYYREAFSE GPCASQGFKS LYQNLQVRAE
GNQLFIEGSE AIDKEHFKKN HLPNLAKQLE KFGFPTFNCQ VEKNDVLTQE QEEAFHAENE
QIVQAANEEA LRAMEQLEQM APPPAEEKPV FDFQAKKAAA KPKLDKAEIT PMIEVTTEEN
RLVFEGVVFD VEQKVTRTGR VLINFKMTDY TSSFSMQKWV KNEEEAQKFD LIKKNSWLRV
RGNVEMNNFT RDLTMNVQDL QEVVHYERKD LMPEGERRVE FHAHTNMSTM DALPEVEEIV
ATAAKWGHKA VAITDHGNVQ SFPHGYKAAK KAGIQLIYGI EANIVEDRVP IVYNEVEMDL
SEATYVVFDV ETTGLSAIYN DLIQVAASKM YKGNVIAEFD EFINPGHPLS AFTTELTGIT
DDHVKNAKPL EQVLQEFQEF CKDTVLVAHN ATFDVGFMNA NYERHDLPKI SQPVIDTLEF
ARNLYPEYKR HGLGPLTKRF GVALEHHHMA NYDAEATGRL LFIFIKEVAE KHGVTDLARL
NIDLISPDSY KKARIKHATI YVKNQVGLKN IFKLVSLSNT KYFEGVSRIP RTVLDAHREG
LILGSACSEG EVFDVVVSQG VDAAVEVAKY YDFIEVMPPA IYAPLIAKEQ VKDMEELQTI
IKSLIEVGDR LGKPVLATGN VHYIEPEEEI YREIIVRSLG QGAMINRTIG HGEHAQPAPL
PKAHFRTTNE MLDEFAFLGE ELARKLVIEN TNALAEIFEP VEVVKGDLYT PFIDKAEETV
AELTYKKAFE IYGNPLPDIV DLRIEKELTS ILGNGFAVIY LASQMLVQRS NERGYLVGSR
GSVGSSFVAT MIGITEVNPL SPHYVCGQCQ YSEFITDGSY GSGFDMPHKD CPNCGHKLSK
NGQDIPFETF LGFDGDKVPD IDLNFSGEDQ PSAHLDVRDI FGEEYAFRAG TVGTVAAKTA
YGFVKGYERD YGKFYRDAEV ERLAQGAAGV KRTTGQHPGG IVVIPNYMDV YDFTPVQYPA
DDVTAEWQTT HFNFHDIDEN VLKLDVLGHD DPTMIRKLQD LSGIDPNKIP MDDEGVMALF
SGTDVLGVTP EQIGTPTGML GIPEFGTNFV RGMVDETHPT TFAELLQLSG LSHGTDVWLG
NAQDLIKQGI ADLSTVIGCR DDIMVYLMHA GLEPKMAFTI MERVRKGLWL KISEEERNGY
IEAMKANKVP EWYIESCGKI KYMFPKAHAA AYVMMALRVA YFKVHHPIYY YCAYFSIRAK
AFDIKTMGAG LEAIKRRMEE ISEKRKNNEA SNVEIDLYTT LEIVNEMWER GFKFGKLDLY
RSQATEFLID GDTLIPPFVA MDGLGENVAK QLVRAREEGE FLSKTELRKR GGLSSTLVEK
MDEMGILGNM PEDNQLSLFD ELF
