ID A0A0R1K2D0_9LACO Unreviewed; 1444 AA.
AC A0A0R1K2D0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=DNA polymerase III PolC-type {ECO:0000256|HAMAP-Rule:MF_00356};
DE Short=PolIII {ECO:0000256|HAMAP-Rule:MF_00356};
DE EC=2.7.7.7 {ECO:0000256|HAMAP-Rule:MF_00356};
GN Name=polC {ECO:0000256|HAMAP-Rule:MF_00356};
GN ORFNames=FD30_GL001987 {ECO:0000313|EMBL:KRK77472.1};
OS Levilactobacillus namurensis DSM 19117.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=1423773 {ECO:0000313|EMBL:KRK77472.1, ECO:0000313|Proteomes:UP000051162};
RN [1] {ECO:0000313|EMBL:KRK77472.1, ECO:0000313|Proteomes:UP000051162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19117 {ECO:0000313|EMBL:KRK77472.1,
RC ECO:0000313|Proteomes:UP000051162};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- FUNCTION: Required for replicative DNA synthesis. This DNA polymerase
CC also exhibits 3' to 5' exonuclease activity.
CC {ECO:0000256|ARBA:ARBA00003452, ECO:0000256|HAMAP-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;
CC Evidence={ECO:0000256|ARBA:ARBA00024632, ECO:0000256|HAMAP-
CC Rule:MF_00356};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00356}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. PolC
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00356}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRK77472.1}.
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DR EMBL; AZDT01000006; KRK77472.1; -; Genomic_DNA.
DR STRING; 1423773.FD30_GL001987; -.
DR PATRIC; fig|1423773.3.peg.2033; -.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000051162; Unassembled WGS sequence.
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; cd07309; PHP; 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; 2.
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; IPR004365; NA-bd_OB_tRNA.
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; 1.
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 Pfam; PF01336; tRNA_anti-codon; 1.
DR SMART; SM00479; EXOIII; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00356};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_00356};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|HAMAP-Rule:MF_00356};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_00356};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00356};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00356};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00356};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 338..405
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 423..589
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
FT REGION 200..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1444 AA; 161847 MW; EDA546AA82109B80 CRC64;
MDEDRHSLFQ KLLQQLDLTS MADQPAFQGA TLNKLTVHDQ SRRWHFYLQF PQILPFTLFA
DFHQHLQIAF HEIATVGATM IVAEPELTNR LLGDYWQWVV KNSGLTNNLV MELTQSQVPE
LDADGRVLLY AQNEVVKDFL QNQALGPLEA TYRQAGFPKF NIQVMVDESK SQAKINEFKA
RQEKTDAQLA KQAAAAIAKA NQKRQSDEPV AASGPTQIGK TIKGDQPVMR MVDITQEERS
VIVEGYVFDK EIRKLRSGRQ LLTLKITDYT SSIVVKKFSR GAEDEAQFAG VSEGSWVKVR
GSVQEDSFMR DLALNAYDIN EVKHASRQDT APADQKRVEL HLHTTMSQMD ATNPIGDFVG
QAKKWGMPAI GITDHADVQG FPAAFNAASK AGVKMLYGVE ANLVDDGVPI GYNSAHVPLD
GATYVVFDVE TTGLSAIYDK VIELSAVKMQ HKNVIDQFEE FIDPGFPLSE QTTNLTSITD
DMVAGSKTEE EVFKLFRDFC GDAIIVGHNV TFDVGFMNTG YQRHGMPEIS NPIIDTLTLA
RWLYPTLKSY RLNTLAKRFH VSLEHHHRAV YDAESTGHLN YLFLKDAEER YHVQFHDQLN
DHMTDNDAYK HARPNHAIIY AQTQAGLKNL FKLVSASNVD YFYRVPRVPR SVLDHYREGL
LVGSACASGE VFTAMMQKGQ VEAAAKAKYY DYLEVQPPQA YQPLLESKLI ADKEHLYEIL
KNMIQLGHDL NKPVVATGDV HYLNPVDAIY RKILIHSQGG ANPLNRQELP PVPFLSTDEM
LKQFDFLDDQ TAHEIVVTNT QKIADQIDDI HPLKDKLYTP RMEGAEDEIR ERTMNTAHAW
YGDPLPELVQ HRVDRELKSI IGNGFSVIYL IAQRLVAKSN KDGYLVGSRG SVGSSVVATL
TGITEVNPLP PHYRCPNCQY SHFYTKGEYS SGYDLPEKKC PKCGTLMIGD GHNIPFETFL
GFKGNKVPDI DLNFSGDYQP IAHNYTKVLF GEKNVYRAGT IGTVADKTAY GYVKAYERDT
EQTFRGAEVD RLAKGATGVK RTTGQHPAGI IVVPDYMDIY DFTPIQYPAD DQNAAWQTTH
FDFHSIHDNI LKIDILGHDD PTMIRMLQDL SGVDPTTIPM DDPGVMGLFS GTDSLGVTPE
QIQSKTGTLG VPEFGTRFVR GMLEQTHPQN YSQLLQISGL SHGTDVWLGN ADELIKNGTA
TIANVIGCRD NIMTDLINYG LDSETSFQIM EQVRHGRGIK DEWQEKMRET DVPEWYIDSC
LKIKYMFPRA HAAAYVLMAL RVAYFKVYFP IIYYAAYFSV RADDFDVVAM SQGKTAVKAA
MKAINDQGMD ASAKDKNLLT VLELANEMLE RGYEFKMIDL EKSDAADWII EGKTLIAPFR
AAPGLGLNVA KQIVAARNDR PFISKEDLAK RGKVSKTLID FMTENGVLTG LPDENQLSLF
DDMM
//
