ID   DPO3_STAA1              Reviewed;        1438 AA.
AC   A7X1P4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=SAHV_1254;
OS   Staphylococcus aureus (strain Mu3 / ATCC 700698).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=418127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu3 / ATCC 700698;
RX   PubMed=17954695; DOI=10.1128/aac.00534-07;
RA   Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.;
RT   "Mutated response regulator graR is responsible for phenotypic conversion
RT   of Staphylococcus aureus from heterogeneous vancomycin-intermediate
RT   resistance to vancomycin-intermediate resistance.";
RL   Antimicrob. Agents Chemother. 52:45-53(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; AP009324; BAF78137.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7X1P4; -.
DR   SMR; A7X1P4; -.
DR   KEGG; saw:SAHV_1254; -.
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; 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_1000048478"
FT   DOMAIN          422..578
FT                   /note="Exonuclease"
SQ   SEQUENCE   1438 AA;  162693 MW;  7E592D300D6708A5 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 TNARKLYGED
     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