DPO3_STAHJ
ID DPO3_STAHJ Reviewed; 1438 AA.
AC Q4L5W6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 129.
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=SH1650;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE04959.1; -; Genomic_DNA.
DR RefSeq; WP_011275936.1; NC_007168.1.
DR AlphaFoldDB; Q4L5W6; -.
DR SMR; Q4L5W6; -.
DR STRING; 279808.SH1650; -.
DR EnsemblBacteria; BAE04959; BAE04959; SH1650.
DR KEGG; sha:SH1650; -.
DR eggNOG; COG2176; Bacteria.
DR HOGENOM; CLU_003297_2_0_9; -.
DR OMA; YYAAYFT; -.
DR OrthoDB; 561611at2; -.
DR Proteomes; UP000000543; 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_1000048481"
FT DOMAIN 422..578
FT /note="Exonuclease"
SQ SEQUENCE 1438 AA; 162950 MW; A8B8460D488D2AE5 CRC64;
MAMTNQEKFK VLADQIKVSN QLDQTIIEKG ELTRVDVSNK NRTWEFQITL PYFLSHEDYL
IFTNAITEEF KEIAKVDWHF TIQDTSNQDE HAIKYFGHCI EHTALSPKVK GQLKQKRLIM
SGNVLKVMTS NDIERNHFDK VCNGSLVKAF RKCGFDIDKV VFETDDSSSY DDLASLEAHI
QEEDEKSARE ATEKIEKIKA EKAKQQDNNE SNVDKCQIGK PIQIDNIKPI ESIIEEEFKV
AIEGVIFDIN LKELKSGRHI VELKVTDYTD SLVLKMFTRK NKDDLDHFKA LSVGKWVRAQ
GRIEEDTFVR DLVMMMTDIE EIKKTPKQDK AEEKRVEFHL HTSMSQMDGI PNISAYVNQA
AKWGHKAIAV TDHNVVQAFP DAHGAAEKNG IKMIYGMEGM LVDDGVPIAY KPTDRDLKEA
TYVVFDVETT GLSNQYDQII ELAAVKVKDG EIIDKFERFS NPHEKLSETI INLTHITDDM
LTDAPEIEEV LTEFKEWVGD AIFVAHNASF DMGFIDTGYE RLGFGPSTNG VIDTLELSRT
INTEYGKHGL NFLAKKYGVE LTQHHRAIYD TESTAYIFIK MVQQMKELGV TNHKDINQKL
SNEDAYKRAR PTHVTLIVQT QEGLKNLFKI VSASLVKYYY RTPRIPRSLL NEYREGILVG
TACDEGELFT AVMQRDQSEV EKIAKYYDFI EVQPPKLYQD LIDRELIRDT ETLYEIYERI
LKAGESTGIP VIATGNAHYL YEHDAIARKI LIASQPGNPL NRSTLPEAHF RTTDEMLDEF
HFLGEEKAHE IVVKNTNELA DRIEKVIPIK DQLFTPRMDG ANEEIRELSY TNAKKLYGED
LPQIVIDRLE KELASIIGNG FSVIYLISQR LVKKSLDDGY LVGSRGSVGS SFVATMTEIT
EVNPLPPHYI CPNCKTSEFF DDGSVGSGFD LPDKQCSTCG AELIKEGQDI PFETFLGFKG
DKVPDIDLNF SGEYQPNAHN YTKVLFGEDK VFRAGTIGTV AEKTAFGYVK GYLNDQGIHK
RGAEIDRLVK GCTGVKRTTG QHPGGIIVVP DYMDIYDFTP IQYPADDQSA SWMTTHFDFH
SIHDNVLKLD ILGHDDPTMI RMLQDLSGID PKTIPVDDKE TMQIFSSPES LGVTEEEILC
KTGTFGVPEF GTGFVRQMLE DTKPTTFSEL VQISGLSHGT DVWLGNAQEL IRSGICDLSS
VIGCRDDIMV YLMYAGLEPS MAFKTMESVR KGKGLTEEMI DAMKENNVPD WYLDSCLKIK
YMFPKAHAAA YVLMAVRIAY FKVHHPLYYY ASYFTIRASD FDLITMIKDK ESIKNTVKDM
YSRYMDLGKK EKDVLTVLEI MNEMAHRGFR MQPISLEKSQ AFDFIIEGDT LIPPFISVPG
LGENVAKRIV EAREDGPFLS KEDLNKKAGL SQKIIEYLDD LGSLPNLPDK AQLSIFDM
