DPO3_LIGS1
ID DPO3_LIGS1 Reviewed; 1444 AA.
AC Q1WUF9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=LSL_0567;
OS Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=362948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCC118;
RX PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K.,
RA Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.;
RT "Multireplicon genome architecture of Lactobacillus salivarius.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(2006).
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; CP000233; ABD99376.1; -; Genomic_DNA.
DR RefSeq; WP_011475822.1; NC_007929.1.
DR RefSeq; YP_535459.1; NC_007929.1.
DR AlphaFoldDB; Q1WUF9; -.
DR SMR; Q1WUF9; -.
DR STRING; 362948.LSL_0567; -.
DR EnsemblBacteria; ABD99376; ABD99376; LSL_0567.
DR KEGG; lsl:LSL_0567; -.
DR PATRIC; fig|362948.14.peg.646; -.
DR HOGENOM; CLU_003297_0_0_9; -.
DR OMA; YYAAYFT; -.
DR Proteomes; UP000006559; 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; IPR016195; Pol/histidinol_Pase-like.
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; SSF50249; SSF50249; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF89550; SSF89550; 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; Reference proteome;
KW Transferase.
FT CHAIN 1..1444
FT /note="DNA polymerase III PolC-type"
FT /id="PRO_1000048474"
FT DOMAIN 426..582
FT /note="Exonuclease"
SQ SEQUENCE 1444 AA; 164253 MW; 00568E498EC1FD8D CRC64;
METNKQDLFK KLLRQINWEN KHGFEEVFTN AEIQKVEVHV ESKVWNFHLQ IEDILPYEVF
YQFYQQLQLA FKDIAKVDIT LHTKNPIITN QKLGDYWKWV VFNSGIQSSF IQELSRSKVP
YLDNNRVILL AENEIVKRFL VDQALGPLES TYHKIGFPKF SVNTLVDETK AQEIIENIKE
QKAKSDAELA QKAVEAIKKQ SEQREKSKAE VPSIEGPVQL GKKISPDQEI TQMINITEEE
RSVTVQGYVF DKEVRELRSG RKLLILEVTD YTASFVVKKF SRTEEDEAMF DAINSGVWIK
VRGSVQEDNY MRDLVINAYD LNEIKHESRK DTAPENEKRV ELHLHSNMSM MDATNSITEY
VSKAAEWGHK AIAITDHGTL QAFPEAHAAG QKNNVKILYG VEANIVDDGV PIAYNEQHKN
LRDATYVIFD TETTGLSAQY DKVIELAAVK MEKGNVIDTF EEFIDPGHPL SQTTINLTSI
TDDMVRGSKS EEEVFRLFKE FCKDCIIVGH NATFDVDFMN TGYERHNMEM IQEPWIDTLP
LARYLYPEMK GFRLNTLAKK LNIKLEHHHR AIYDAEATGF IYYAMLKDAE EKQILYHDDF
NKHVGENDAY KHEHPSHAII LAKTQEGLKN LFKLTSESMV KYFYRVPRVP RSILEKYREG
LIVGSACADG EVFTAMMQKG YTIAKQKAEF YDYLEVQPKP LYEPLLEQEL VKDNDNLEEI
ITNMVKLAHE LDKPIVATGD VHFMNKEDAI YRKILIHSQA GANPLNRLKK LPDAHFRTTD
EMLEEFSFLG EDIAKEIVVT NPNKLVDEIS EITPVKDKLY TPKMEGAEQD IHDLTMNRAH
AWYGDTLPEI VQKRLDKELK SVIGNGFSVI YLISQKLVYK SNKDGYLVGS RGSVGSSLVA
TMTGITEVNP LPPHYRCPKC KWTHFYEKGE YGSGYDLPDK DCPNCGTELI KDGQDIPFET
FLGFKGNKVP DIDLNFSGDY QPIAHNYTKV LFGENNVYRA GTIGTVADKT AYGYVKAYER
DTEQNFRGAE IDRLAKGATG VKRTTGQHPA GILVVPDYMD IYDFTPIQYP ADDLTAAWRT
THFDFHSIHD NILKLDILGH DDPTMIRMLQ DLSGIDPKTI PTDDPGVMAL FSGTDILGVT
PEEIQSSTGT LGVPEFGTRF VRGMLEETHP KTFAELLKIS GLSHGTDVWL GNAEELIKNG
TVTMPDVIGC RDDIMMDLIH MGVESDKAFK IMEHVRKGRG IPDEWQADMR AADVPEWYIG
ACLKIKYMFP KAHAAAYVLM ALRIAYFKVY YPLVYYAAYF SVRADDFDLV SMSRGKEAVK
NAMELINSKG NEATTKEKNL LTVLEIANEM LERGFDFSMV DINKSDAQNW TIQEDGRTLL
APFTAIPGLG LNVAKQIVAA REEQEFISKE DLSKRGKVSQ SLIDFMTENH VLDDLPDENQ
LSLF
