ID A8FDC2_BACP2 Unreviewed; 1437 AA.
AC A8FDC2;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 108.
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 ECO:0000313|EMBL:ABV62239.1};
GN OrderedLocusNames=BPUM_1557 {ECO:0000313|EMBL:ABV62239.1};
OS Bacillus pumilus (strain SAFR-032).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=315750 {ECO:0000313|EMBL:ABV62239.1, ECO:0000313|Proteomes:UP000001355};
RN [1] {ECO:0000313|EMBL:ABV62239.1, ECO:0000313|Proteomes:UP000001355}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV62239.1,
RC ECO:0000313|Proteomes:UP000001355};
RX PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA Weinstock G.M.;
RT "Paradoxical DNA repair and peroxide resistance gene conservation in
RT Bacillus pumilus SAFR-032.";
RL PLoS ONE 2:E928-E928(2007).
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}.
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DR EMBL; CP000813; ABV62239.1; -; Genomic_DNA.
DR STRING; 315750.BPUM_1557; -.
DR KEGG; bpu:BPUM_1557; -.
DR eggNOG; COG2176; Bacteria.
DR HOGENOM; CLU_003297_2_0_9; -.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000001355; 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 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; 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 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 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 335..402
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 420..587
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
FT COILED 180..207
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1437 AA; 162960 MW; 05E730E5958325FE CRC64;
MDEQLPITRR QFHILLNQIQ MTDDDLSRYF EEGEIVKLTV HKLAKTWHFL FKFKALLPYK
VYAMFLSRLT NAFSHIAQVT CTIEVNDPSI SEELVQSYWS HCVEELQGIS PPIISLLQQQ
KPSLSGHKII IKTKSETEAL AIKKKYSPML QAAFKQVGFP ELQFDTEIFV SDQEIQKFRE
QKLAEDQERA MQALTEMEKK ESEEQEEGPS GPLMIGYQIK DNEEIRTLDS IMDEERRITV
QGYVFDAETR ELKSGRTLCI FKITDYTNSI LIKMFAREKE DAQLMKSLKK GMWVKARGSI
QNDTFVRDLV MIANDVNEMK PQLKEDTAPE GEKRVELHLH SPMSQMDAVT GIGRLVEQAK
KWGHEAIALT DHAVVQSFPD AYAASRKHDI KMMYGVEINL VDDGVPIAYN PEHRLLEDAT
YVVFDVETTG LSAVYDTIIE LAAVKIKGGE IIDRFEAFAN PHHPLSATTI ELTGITDDMV
RDAPDVVDVV RDFKEWIGQD ILVAHNASFD MGFLNTAYKR LLKTDKASNP VIDTLELGRF
LYPEFKNHRL NTLCKKFDIE LTQHHRAIYD AEATGYLMLK MLKDAAEKDI AYHDQLNENM
GQSNAYQRSR PYHAILIAQN ETGLKNLFKL VSLSHIHYFY RVPRIPRSQL EKYREGLIIG
SACDKGEVFE GMMQKSPDEV EDIAAFYDYL EVHPPEVYQH LLQLELVRDE RALKEIITNI
VKLGEKLNKP VVATGNVHYL HPEDKIYRKI LISSQGGANP LNRHELPKVH FRTTDEMLEA
FSFLGEEKAK EIVVTNTKKV SEMVESIKPI KDDLYTPKIE GADEEIREMS YQMARSIYGD
DLPKIVEDRI EKELKSIIGH GFAVIYLISH KLVKKSLDDG YLVGSRGSVG SSLVATLTEI
TEVNPLAPHY VCPSCKHSEF FNDGSVGSGF DLPDKDCPEC GTPYKKDGHD IPFETFLGFK
GDKVPDIDLN FSGEYQPIAH NYTKELFGEE YVYRAGTIGT VAEKTAYGYV KGYAGDHNLH
MRGAEIDRLV QGCTGVKRTT GQHPGGIIVV PDYMDIYDFS PIQFPADATG SDWKTTHFDF
HSIHDNLLKL DILGHDDPTV IRMLQDLSGI DPKTIPTDDP EVMKIFQGTE PLGVTEEQIG
CKTGTLGIPE FGTRFVRQML EDTKPTTFSE LVQISGLSHG TDVWLGNAQE LIHNKTCELS
EVIGCRDDIM VYLIYQGLEP SLAFKIMESV RKGKGLPPEW EEEMKNNNVP NWYIDSCKKI
KYMFPKAHAA AYVLMAVRIA YFKVHHALLY YAAYFTVRAD DFDIETMTKG SNAIRAVMDD
INSKGLDASP KEKNLLTVLE LALEMCERGY HFKKVDLYRS SATEFIIDGD GLIPPFNSIP
GLGTNVALNI VRARQDGEFL SKEDLQKRGK VSKTILEYLD RQGCLEALPD QNQLSLF
//
