ID   DPO3_STAAB              Reviewed;        1438 AA.
AC   Q2YXK4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-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=SAB1126;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(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; AJ938182; CAI80815.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2YXK4; -.
DR   SMR; Q2YXK4; -.
DR   KEGG; sab:SAB1126; -.
DR   HOGENOM; CLU_003297_0_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_1000048480"
FT   DOMAIN          422..578
FT                   /note="Exonuclease"
SQ   SEQUENCE   1438 AA;  162656 MW;  97DA5607AC383458 CRC64;
     MAMTEQQKFK VLADQIKISN QLDAEILNSG ELTRIDVSNK NRTWEFHITL PQFLAHEDYL
     LFIHAIEQEF 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 LVDDGAPIAY KPQDVVLKDA
     TYVVFDVETT GLSNQYNKII ELAAVKVHNG EIIDKFERFS NPHERLSETI INLTHITDDM
     LVDAPEIEEV LTEFKEWVGD AIFVAHNASF DMGFIDTGYE RLGFGPSTNG VIDTLELSRT
     INTEYGKHGL NFLAKKYGVE LTQHHRAIYD TEATAYIFIK MVQQMKELGV LNHNEINKKL
     SNQDAYKRAR 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