ID DPO3_STAS1 Reviewed; 1438 AA.
AC Q49X49;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, 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=SSP1504;
OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS 20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=342451;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT pathogenesis of uncomplicated urinary tract infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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; AP008934; BAE18649.1; -; Genomic_DNA.
DR RefSeq; WP_011303258.1; NZ_MTGA01000034.1.
DR AlphaFoldDB; Q49X49; -.
DR SMR; Q49X49; -.
DR KEGG; ssp:SSP1504; -.
DR PATRIC; fig|342451.11.peg.1506; -.
DR eggNOG; COG2176; Bacteria.
DR HOGENOM; CLU_003297_2_0_9; -.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000006371; 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 CDD; cd06127; DEDDh; 1.
DR CDD; cd07435; PHP_PolIIIA_POLC; 1.
DR CDD; cd04484; polC_OBF; 1.
DR Gene3D; 1.10.150.870; -; 1.
DR Gene3D; 3.30.1900.20; -; 2.
DR Gene3D; 6.10.140.1510; -; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 1.10.150.700; PolC, middle finger domain; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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; IPR004805; DnaE2/DnaE/PolC.
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; Pol_III_a_PolC-type_gram_pos.
DR InterPro; IPR044923; PolC_middle_finger_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR NCBIfam; TIGR00573; dnaq; 1.
DR NCBIfam; TIGR01405; polC_Gram_pos; 1.
DR PANTHER; PTHR32294:SF5; DNA POLYMERASE III POLC-TYPE; 1.
DR PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 1.
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; 2.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00479; EXOIII; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF81585; PsbU/PolX domain-like; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm; DNA replication; DNA-directed DNA polymerase; Exonuclease;
KW Hydrolase; Nuclease; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..1438
FT /note="DNA polymerase III PolC-type"
FT /id="PRO_1000048482"
FT DOMAIN 422..578
FT /note="Exonuclease"
SQ SEQUENCE 1438 AA; 162441 MW; 7CD4F6D814A2510C CRC64;
MAMTNEEKFK ILADQIKITE HLDSEILENS ELTRVDVKTS DRTWVFQITF PHFLTIENYL
LFTGAIIEEF KTIADVKCNF TVKDKTNQDE FAIKYFSHCI DQTKLSPKVK GQLKQKRLIM
SGDVLKVMCQ NDVERDHFDK ACNGSLIAAY QQCGFNISKV VFETDSAVND GDLASLEAHI
QEEDEKSARE ATEKLEKMKA EKAKQQDNNE SDVSKCQIGK PIQVENVRQI DSIIEEEFKA
AVEGVIFDIN LKELKSGRHI VELKVTDYTD SLVLKMFTRK NKDDLAHFKA LSVGKWVRAQ
GRIEEDTFVR DLVMMMSDIE EIKKATKQDK AEDKRVEFHL HTSMSQMDGI PNISDYVDQA
AKWGHKAIAV TDHNVVQAFP DAHSAAEKNG IKMIYGMEGM LVDDGVPIAY KPKDCDLKTA
TYVVFDVETT GLSNQYDKII ELAAVKVKDG EIIDKFERFS NPHERLSETI KNLTHISDDM
LVDAPEIEEV LTEFKSWVGD AIFVAHNASF DMGFIDTGYE HVGIGASTNG VIDTLELSRT
INTEYGKHGL NFLAKKYGVE LTQHHRAIYD TEATAYMFIK MLKQLEALGV HNHQDINTSL
SNEDAYKRAR PNHVTLIVQN QDGLKNLFKI VSASLVQYYY RTPRIPRSLL DEYREGILVG
SACDEGEVFT AVMQKDQSQV ERIAKYYDFI EVQPPALYQD LIDRELVRDN ETLHEIYNRL
IRAGDVNNIP VIATGNAHYL NEHDAIARKI LIAAQPGNPL NRSTLPKAHF RTTDEMLDEL
HFLGEEKAYE LVVQNTNDLA DKIERVVPIK DELFTPRMEG ANEEIREMSY DNAKALYGDD
LPQIVIDRLE KELESIIGNG FSVIYLISQR LVKKSLNDGY LVGSRGSVGS SFVATMTEIT
EVNPLPPHYI CPECKQSEFF DDGSVGSGFD LPDKKCESCG CDLIKEGQDI PFETFLGFKG
DKVPDIDLNF SGEYQPEAHN YTKELFGEDK VFRAGTIGTV AEKTAFGFVK GYLNDQGIHK
RGAEIDRLVK GCTGVKRTTG QHPGGIIVVP DYMDIYDFTP VQFPADDQGS SWMTTHFDFH
SIHDNVLKLD ILGHDDPTMI RMLQDLSGID PKTIPVDDKE TMGIFSSPEP LGVTSDEILC
KTGTFGVPEF GTGFVRQMLE DTKPTTFSEL VRISGLSHGT DVWLGNAQDL IRSGKCDLAS
VICCRDDIMV YLMYNGLEPS LAFKTMEFVR KGKGLTDDMV EAMVDNEVPD WYLDSCRKIK
YMFPKAHAAA YVLMAVRIAY FKVHYPLYYY ASYFTVRASD FDLISMIKDK ESIRNTVNDM
YSRYMDLAKK EKDTLTVLEI MNEMAQRGYR MQPISLEKSK AFEFIIEGDT LIPPFIAVPG
LGENVAQRIV EARDEGPFLS KEDLNKKAGL SQKVIEYLDE LGSLPNLPDK AQLSIFDM
//
