ID A0A0R1QWT6_9LACO Unreviewed; 1446 AA.
AC A0A0R1QWT6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=FD01_GL000576 {ECO:0000313|EMBL:KRL45803.1};
OS Lacticaseibacillus manihotivorans DSM 13343 = JCM 12514.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1423769 {ECO:0000313|EMBL:KRL45803.1, ECO:0000313|Proteomes:UP000051790};
RN [1] {ECO:0000313|EMBL:KRL45803.1, ECO:0000313|Proteomes:UP000051790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13343 {ECO:0000313|EMBL:KRL45803.1,
RC ECO:0000313|Proteomes:UP000051790};
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: DNA polymerase III is a complex, multichain enzyme
CC responsible for most of the replicative synthesis in bacteria. This DNA
CC polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain
CC is the DNA polymerase. {ECO:0000256|ARBA:ARBA00025611}.
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. DnaE
CC subfamily. {ECO:0000256|ARBA:ARBA00009496}.
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:KRL45803.1}.
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DR EMBL; AZEU01000116; KRL45803.1; -; Genomic_DNA.
DR RefSeq; WP_056963288.1; NZ_AZEU01000116.1.
DR PATRIC; fig|1423769.4.peg.612; -.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000051790; 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; 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; 1.
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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000051790};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 336..403
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 422..588
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
FT REGION 200..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 168..200
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1446 AA; 161133 MW; 1FE8406B966176C4 CRC64;
MALSKHEMFT KLLEQLQLPQ DLANYPGFND ATIDQVAVHT KSKHYHFTIG VPTILPVAVY
TPFEQHLQAA FKDIASVGLS IKAENPSFDQ ALLSGYWAYV VKNAGIQSSL VYELCTKQEP
KLNDGRVSLL AENEPVRQFL INQGLGKLED AYHTVGFQTL HLNADVDEDK ANAQIEAFKA
QKAQETAELA KKAAEVVQQR QQAQAADPNA GSGPITLGRG IKSSDEPQQM VTITEEERSV
TVEGYVFDVE VRELRSKRKL LIFKLTDYTS SFIAKKFSNN AEDEAMFDRI SAGMWLRVRG
SVQEDNFSRE LTIMAQDVQE VKHPLPTDDV EGDKRIELHL HTNMSTMDGM TSISDYVKRA
KKWGHEAIAV TDHAGLQAYP EAHTAAGKAD MKMIYGVEVN LVDDGTPVAY NADVARPLAT
DTYVVFDIET TGLSAVYDKI IEIAAVKMQD GKVIDEFEEL IDPGFPLSEF TINLTHITDD
MVHGSKTEAQ VLNLFREFCD GSIMVGHNVT FDVGFINAGY RRLNQEDIQN PVVDTLELSR
MLHPERKNHK LDTLTKAYKI ALENHHRANA DSEATGYLLY ALEKEAAKKY NITTLDQLNS
RVGAGDAWKQ SRPSHAIILA KTQEGLKNLF KLVSISNVET YYRMPRVPRS RLQKLRDGLV
VGSACSSGEV FTAMMQKGYA EAAKKAEFYD YLEVQPLDNY LPLKEAELVK GDAHLKDIIS
NIIKIGAAQN KPVVATGDAH YLDKTDAVYR KILIHSQGGA NPLNRHSLPD VHFRSTKEML
DAFSWLPEDQ AHQIVVDNTH VVADWIDGSI TPVKTKLYTP DIPGVKENLT KDVMDTAHKL
YGDPLPEIVS ARLDKELKSI IGNGFAVIYN IAQQLVLKSN KDGYLVGSRG SVGSSLAATM
SGITEINPLP PHYRCPQCQY SEFFTKGEYG SGFDLPDKDC PNCGAELVKD GQDIPFETFL
GFKGDKVPDI DLNFSGDYQP VAHNYIKVLF GEDHAFRAGT IGTVADKTAY GYVKAYERDT
GQMIRGAEID RLAKGATGVK RTTGQHPAGI LIVPANMDIY DFSPIQYPAD DQNAAWKTTH
FDFHSIHDNI LKMDVLGHDD PTMIRMLQDL SGVEPKSIPM DDPGVMSLFS STEALGVTPE
QIGSKTGTLG VPEFGTRFVR GMLEETHPKH FSELLQISGL SHGTDVWLGN AEELIQNKVV
TIKEVIGCRD NIMMDLIHWG MDDSMAFNIM EHVRKGRGIP DEWQQAMRDN ESVPDWYIDS
CLKIKYMFPK AHAAAYDLMG LRIAWFKVYF PLVYYASYFS VRAEDFDLAA MSHGKEAVKA
AIKEITDKGM EASTKEKNLQ TILEIANECL ERGFKIQMVD IDKSDAHDFL IVDDHTLLAP
FRAVPSLGDN VAKQIVSARE EKPFLSKEDL AKRGKVSKTL IDYMTENHVL DHLPDENQLS
LFDGLF
//
