ID A0A0R1S0V7_9LACO Unreviewed; 1446 AA.
AC A0A0R1S0V7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=FC69_GL001530 {ECO:0000313|EMBL:KRL59571.1};
OS Latilactobacillus fuchuensis DSM 14340 = JCM 11249.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Latilactobacillus.
OX NCBI_TaxID=1423747 {ECO:0000313|EMBL:KRL59571.1, ECO:0000313|Proteomes:UP000051264};
RN [1] {ECO:0000313|EMBL:KRL59571.1, ECO:0000313|Proteomes:UP000051264}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14340 {ECO:0000313|EMBL:KRL59571.1,
RC ECO:0000313|Proteomes:UP000051264};
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|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:KRL59571.1}.
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DR EMBL; AZEX01000044; KRL59571.1; -; Genomic_DNA.
DR RefSeq; WP_056950445.1; NZ_AZEX01000044.1.
DR STRING; 1423747.FC69_GL001530; -.
DR PATRIC; fig|1423747.3.peg.1558; -.
DR eggNOG; COG2176; Bacteria.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000051264; 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; 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; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
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; SSF160975; AF1531-like; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF89550; PHP domain-like; 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 339..406
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 424..590
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
FT REGION 201..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1446 AA; 161486 MW; CDD784A38CA155F1 CRC64;
MALDQTALFQ KLLEQIELPA DVANYPGFKT GQVEQVIVHE TSKAWTFKLH FETVLPYAVF
VTFEQYLEAA FKSIATVQLA MTTDKTELDG GVLAAYWEYV VNHSGIQSSL LHELCAKETP
YMDGKQTYLV VENDIVKNFF INQAQTAIQD GYRRLGFPKF AIQPLIDESA SQKAIEDFQA
KKAVQDAARA QAAAEAIKKN EALKEKRQAE GKPVDGPISM GRGLKPDEPA RQMITINEEE
RSVVIEGYVF DKEVRVLRSG RQLLILKMTD YSSSFTVKKF SRDASDEGLF AAINPGMWFK
VRGSVQEDNF LRDLVLNAND LVEVSHPKRQ DTAENGKRVE LHLHTNMSQM DATNKIGDFV
KQAASWGQSA IAVTDHYNLQ SFPDAYAAGK KNNVKILYGV EVNLVNDGTP VAYNLRDEVL
ETAEYVIFDV ETTGLSAVYD SIIELAAVKM KNGEVVASFD EFINPGKSLS AFTTQLTSIT
NEMVQDAKSE AAVLAMFKDF AGDAVLAGHN ITFDMGFLNA GYGRNELGQI ENPVIDTLEL
SRMLHPEYKN HKLDSLTKRY KINLEHHHRA NADAESTGYL LYKLETEAAT RYEMLNVNQL
NNRVGEGDSY KQARPAHAVL MAKTQAGLKN LFKLVSASMT EYYYRTPRLP KSRLDALREG
IIVGSACSSG EVFEAMMQKG YEEARSRAKY YDYIEVMPKA VYAPLLEREL VQDEKALEEI
IANLVKLGAE LGKPVVATGD AHYLNPVDSI YRKILINSMG GANPLNRSKL PDVHFRSTDE
MLKAFAFLGA DKAQEIVVTN PNALADSLDE IVPVKDKLYT PKMEGAEDEI QTLTMNRAHE
LYGAELPVIV QERLDKELKS IIGNGFSVIY LISQKLVYKS GKDGYLVGSR GSVGSSLVAT
MTGITEVNPL PPHYRCPNCH YSEFYTKGEV GSGYDLDDKN CPQCDTPLDK DGHDIPFETF
LGFHGDKVPD IDLNFSGDYQ SVAHNYTKVL FGENNVFRAG TIGTVADKTA YGYVKAYERD
TEQTFRAAEI DRLAKGSTGV KRTTGQHPAG IIVVPDYMDI YDFTPIQFPA DDQDAAWKTT
HFDFHSIHDN ILKLDILGHD DPTMIRMLQD LSGINPKTIP TDDPGVMALF SGTDSLDVTP
EQINSKMGTL GVPEFGTRFV RGMLEETHPT TFSELLQISG LSHGTDVWLG NAEELINKGV
VTLKDVIGCR DNIMMDLIHW GMDDSIAFNI MERVRKGKGI PDDWQQAMRE NENVPDWYID
SCLKIKYMFP KAHATAYIMM ALRIAYFKVY FPIIYYCTYF SVRADDFDLV AMAQGKEGVK
ARMKEITDKG MEASTKEKNL LTVLEIANEC LERGINIKMV DVEKSDSANF LIQDDHTLLA
PFRAVPGLGD NVAKQIVSAR EEKPFLSKED LSNRGKVSKT LIEYMTVNNV LSDLPDENQL
SLFDMM
//
