DPO3_STAAE
ID DPO3_STAAE Reviewed; 1438 AA.
AC A6QGG4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=NWMN_1174;
OS Staphylococcus aureus (strain Newman).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=426430;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Newman;
RX PubMed=17951380; DOI=10.1128/jb.01000-07;
RA Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT analysis of staphylococcal genomes: polymorphism and evolution of two major
RT pathogenicity islands.";
RL J. Bacteriol. 190:300-310(2008).
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; AP009351; BAF67446.1; -; Genomic_DNA.
DR AlphaFoldDB; A6QGG4; -.
DR SMR; A6QGG4; -.
DR EnsemblBacteria; BAF67446; BAF67446; NWMN_1174.
DR KEGG; sae:NWMN_1174; -.
DR HOGENOM; CLU_003297_2_0_9; -.
DR OMA; YYAAYFT; -.
DR Proteomes; UP000006386; 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; 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; 2.
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; 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..1438
FT /note="DNA polymerase III PolC-type"
FT /id="PRO_1000072072"
FT DOMAIN 422..578
FT /note="Exonuclease"
SQ SEQUENCE 1438 AA; 162663 MW; 553DEBEB60D419AA CRC64;
MAMTEQQKFK VLADQIKISN QLDAEILNSG ELTRIDVSNK NRTWEFHITL PQFLAHEDYL
LFINAIEQEF KDIANVTCRF TVTNGTNQDE HAIKYFGHCI DQTALSPKVK GQLKQKKLIM
SGKVLKVMVS NDIERNHFDK ACNGSLIKAF RNCGFDIDKI IFETNDNDQE QNLASLEAHI
QEEDEQSARL ATEKLEKMKA EKAKQQDNNE SAVDKCQIGK PIQIENIKPI ESIIEEEFKV
AIEGVIFDIN LKELKSGRHI VEIKVTDYTD SLVLKMFTRK NKDDLEHFKA LSVGKWVRAQ
GRIEEDTFIR DLVMMMSDIE EIKKATKKDK AEEKRVEFHL HTAMSQMDGI PNIGAYVKQA
ADWGHPAIAV TDHNVVQAFP DAHAAAEKHG IKMIYGMEGM LVDDGVPIAY KPQDVVLKDA
TYVVFDVETT GLSNQYDKII ELAAVKVHNG EIIDKFERFS NPHERLSETI INLTHITDDM
LVDAPEIEEV LTEFKEWVGD AIFVAHNASF DMGFIDTGYE RLGFGPSTNG VIDTLELSRT
INTEYGKHGL NFLAKKYGVE LTQHHRAIYD TEATAYIFIK MVQQMKELGV LNHNEINKKL
SNEDAYKRAR PSHVTLIVQN QQGLKNLFKI VSASLVKYFY RTPRIPRSLL DEYREGLLVG
TACDEGELFT AVMQKDQSQV EKIAKYYDFI EIQPPALYQD LIDRELIRDT ETLHEIYQRL
IHAGDTAGIP VIATGNAHYL FEHDGIARKI LIASQPGNPL NRSTLPEAHF RTTDEMLNEF
HFLGEEKAHE IVVKNTNELA DRIERVVPIK DELYTPRMEG ANEEIRELSY ANARKLYGED
LPQIVIDRLE KELKSIIGNG FAVIYLISQR LVKKSLDDGY LVGSRGSVGS SFVATMTEIT
EVNPLPPHYI CPNCKTSEFF NDGSVGSGFD LPDKTCETCG APLIKEGQDI PFETFLGFKG
DKVPDIDLNF SGEYQPNAHN YTKVLFGEDK VFRAGTIGTV AEKTAFGYVK GYLNDQGIHK
RGAEIDRLVK GCTGVKRTTG QHPGGIIVVP DYMDIYDFTP IQYPADDQNS AWMTTHFDFH
SIHDNVLKLD ILGHDDPTMI RMLQDLSGID PKTIPVDDKE VMQIFSTPES LGVTEDEILC
KTGTFGVPEF GTGFVRQMLE DTKPTTFSEL VQISGLSHGT DVWLGNAQEL IKTGICDLSS
VIGCRDDIMV YLMYAGLEPS MAFKIMESVR KGKGLTEEMI ETMKENEVPD WYLDSCLKIK
YMFPKAHAAA YVLMAVRIAY FKVHHPLYYY ASYFTIRASD FDLITMIKDK TSIRNTVKDM
YSRYMDLGKK EKDVLTVLEI MNEMAHRGYR MQPISLEKSQ AFEFIIEGDT LIPPFISVPG
LGENVAKRIV EARDDGPFLS KEDLNKKAGL SQKIIEYLDE LGSLPNLPDK AQLSIFDM