ID A0A0R2DJG4_9LACO Unreviewed; 1438 AA.
AC A0A0R2DJG4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=FC86_GL000910 {ECO:0000313|EMBL:KRN03798.1};
OS Holzapfeliella floricola DSM 23037 = JCM 16512.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Holzapfeliella.
OX NCBI_TaxID=1423744 {ECO:0000313|EMBL:KRN03798.1, ECO:0000313|Proteomes:UP000051378};
RN [1] {ECO:0000313|EMBL:KRN03798.1, ECO:0000313|Proteomes:UP000051378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23037 {ECO:0000313|EMBL:KRN03798.1,
RC ECO:0000313|Proteomes:UP000051378};
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:KRN03798.1}.
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DR EMBL; AYZL01000020; KRN03798.1; -; Genomic_DNA.
DR RefSeq; WP_056975111.1; NZ_AYZL01000020.1.
DR STRING; 1423744.FC86_GL000910; -.
DR PATRIC; fig|1423744.4.peg.935; -.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000051378; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000051378};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 333..400
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 419..586
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
FT REGION 192..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1438 AA; 162862 MW; 9C32037F9050BC2B CRC64;
MSKENQLFLN LLNQVKFNQL VADGFSENDS FYQGQIKKVD VYQQERKWIF HLFFPKKISF
SAYQLLKQAV TQELSSFVEP ELVVAFGEKS DAIDNDYYQD IIEHHLTSSS MIKRILLNSK
SDYQNRVLTL KLENAVSQAM ITDDVLVELT ELLQQHGFLV DQIKITVIDE AQSLKNLDSL
YQQQQQFEQS LEHEAHKQQA APKKQTVTSS QTSLGNPISP KSQFQQLKDI QEEQQDVVIE
GHLFDVEVRS LRNDNKMLIA KITDYSDSIT IKKFPRNQQE TAVFENIKPG MWARVKGQTQ
NDKYSQELTI MIKDFEVFEK PERQDTYDGE KRAELHLHTT MSQMDATNSI KEYVQAAARF
GHKAIAVTDH AGAQAFPEAH AAGQANDVKI LYGQEANFVD DSKNLLVQNP ISLDAQSADY
VIFDVETTGL SAVYDQIIEI GAVRMKNGEI IERFDEFINP HEALSTTTIN LTSITDDMVE
QADDEKDVLT RFVKFMSESE AIAGHNVSFD IGFLNAALVR SGFKKVSIPV IDTLELSRLL
HPEQGRHTLD TLSRKYQITL EHHHRADSDA EATGYLLYKL MTVFDNQFGE TNLDNYNQHK
NPHLTYKRAR PSHMTILAKT QSGLKNLFKL ISMANIKYYY RTPRLPKFLL DDYREGLLIG
SGCADGEVFT AMMQKGYEEA KQLAKYYDYL EIQPPSAYSY LIERELIRNQ ADLQDILKNM
IRLGQELDKP VVVTGDVHYL NPEDHIYREI LISSIKSSPL RHQNLPDLHF RTTQEMFDEF
NFLDEQTAYQ VIVANPNRIA ESTEDIVPVK DKLYTPIMEH SEEEIRELSY NKAYELYGNP
LPQIVEDRIE HELKSIIGNG FSVIYLISQK LVYKSNKDGY LVGSRGSVGS SFAATMTGIT
EVNPLPPHYR CASCKYSEFY TKGEYGSGYD LPNKKCPNCD KELVKDGHDI PFETFLGFKG
DKVPDIDLNF SGDYQPVAHN YTKVLFGEDS VFRAGTIGTV ADKTAFGYVK HYEEEKELDL
RTAEVERLAK GSTGVKRTTG QHPAGIIVVP DYMDIYDFTP IQYPADDQSS TWKTTHFDFH
SIHDNILKLD ILGHDDPTMI RMLQDLSGID PLTIPTNDPG VMALFSGTDS IGVTPEQINS
KTGTLGVPEF GTKFVRGMLE DTKPTTFAEL LQISGLSHGT DVWLGNASDL VDSGQVTLKE
VIGCRDNIML DLIHWGMESQ TAFQIMERVR KGKGIPEEWQ ELMRDNPNIP SWYIDSCLKI
KYMFPKAHAT AYVMMALRIA YFKVHYPTIY YAAYFSVRAS DFDLVAMSNG KNSVKEAMQE
ISAKGNDATA KDKSLMTVLE LANECLERGI KIKMVDVEKS AAQDFTILDD NTLLAPFNAV
PGLGDNVAKQ IVAARADKKF LSQEDLATRG KVSKTIMGYF EENGVLEGLP EQNQLSLF
//
