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Database: UniProt
Entry: D0BKK8_9LACT
LinkDB: D0BKK8_9LACT
Original site: D0BKK8_9LACT 
ID   D0BKK8_9LACT            Unreviewed;      1441 AA.
AC   D0BKK8;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 83.
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=HMPREF0446_00493 {ECO:0000313|EMBL:EEW93611.1};
OS   Granulicatella elegans ATCC 700633.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Granulicatella.
OX   NCBI_TaxID=626369 {ECO:0000313|EMBL:EEW93611.1, ECO:0000313|Proteomes:UP000002939};
RN   [1] {ECO:0000313|EMBL:EEW93611.1, ECO:0000313|Proteomes:UP000002939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700633 {ECO:0000313|EMBL:EEW93611.1,
RC   ECO:0000313|Proteomes:UP000002939};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA   Yandava C., Sibley C.D., Field T.R., Grinwis M., Eshaghurshan C.S.,
RA   Surette M.G., Haas B., Nusbaum C., Birren B.;
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEW93611.1, ECO:0000313|Proteomes:UP000002939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700633 {ECO:0000313|EMBL:EEW93611.1,
RC   ECO:0000313|Proteomes:UP000002939};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., Field T.R.,
RA   Grinwis M., Eshaghurshan C.S., Surette M.G., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Granulicatella elegans ATCC 700633.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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:EEW93611.1}.
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DR   EMBL; ACRF02000013; EEW93611.1; -; Genomic_DNA.
DR   RefSeq; WP_006702767.1; NZ_KI391971.1.
DR   STRING; 626369.HMPREF0446_00493; -.
DR   eggNOG; COG2176; Bacteria.
DR   HOGENOM; CLU_003297_2_0_9; -.
DR   OrthoDB; 9804290at2; -.
DR   Proteomes; UP000002939; 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; 1.
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; 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; 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:UP000002939};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00356}.
FT   DOMAIN          340..407
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
FT   DOMAIN          425..591
FT                   /note="Exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00479"
SQ   SEQUENCE   1441 AA;  163689 MW;  7912BEC55E9908B7 CRC64;
     MSEHQQQLFL TLMNQLQLDN EQFLQPDFDQ ASLTKIDITK SIPEWCFNIE TNHVIQYEKF
     KRFYEQLKQT YEKIAQVRLV VKTREESQIT QEQIQAYWEM VLFQLQQESP LVVQLLSGQI
     PTWNQKKIQF HCPNEITKSH VNENYIKKIQ QYFENFGFPK MGVDIIVNDE LGSQLEEELR
     IKHETIEQEY QEKAVQQKEV QETAASKPAA VNSDSSILYG KAIRSNLETR EIADIYEEER
     NVLVEAQIFD IEIRTRKASG KSFANIKMTD YTSSIGATLF PSTAEDEERL AALKKGTWVK
     AYGNIEINKF SQELNMIVRD MNKVEHIGRI DRAPEDQKRI ELHLHTNMSV MDATNSASDL
     VKQAAKWGHP AVAITDHANL QSYPEAHGAG KGNNIKILYG LEGNIVDDQV NVAYNPQHIL
     LEDATYVVFD VETTGLSAIY DSIIELAAVK MHKGNVIDKF EEFIDPGHPL SATTIQLTGI
     TDDMVRGSKS QAQVLKEFAA FTKDTILVAH NASFDMGFLN TGYEKEGLEK TTQPVIDTLE
     LSRLLHPHLK SHRLNTLAKR YNVALEQHHR AVFDSETTGH LCHIFLKEAA NDHGLIYHDQ
     LNTNLHPEEV FKNGRPFHAT IFAKHQAGLK ELFKVVSASN VQYFYRVPRI LRSMLIENRD
     SFLIGSGCSE GEVFEAMMQK GYEEAKEKAK FYDYIEIMPK AVYRPLIDKE LIRNEHHLEE
     IIKNLVKLGE ELDIPVVATG NVHYLNPEDK IYREILLTSV NNGQKLNYPD VHFRTTNEML
     DEFAFLGEEK AFEVVVTNTH WVNDQLEVII PIKDDLYTPK IEGAEDEITK LSYDKAHEWY
     GEELPEIVEK RIDKELKSII GNGFSVIYLI SQKLVHKSNE DGYLVGSRGS VGSSLVATLT
     GITEVNPLAP HYRCPNCCYS EFFDDGSVGS GFDLPEKDCP KCGTRLAKDG HDIPFETFLG
     FYGDKVPDID LNFSGEYQPQ AHNYTKVLFG EDYVYRAGTI GTVADKTAFG YVKGYERDLG
     LEFRQAEIDR LAKGCTGVKR STGQHPGGII VIPDYMDVYD FTPIQFPADD QNAEWKTTHF
     DFHSIHDNVL KLDILGHDDP TVIRMLQDLS GIEPKDIPPD DPEVMKIFGG TEVLGVTPEQ
     IDSNTGTLGI PEFGTKFVRG MLEQTKPTTF TELLQISGLS HGTDVYLGNA EELIRLHGIP
     LSEVIGCRDD IMVYLIHKGV ENGAAFKIME GVRKGKGIPE DYQAMMRENN VPEWYIESCL
     KIKYMFPKAH AAAYVLMALR VAWFKVHKPL LYYCAYFSVR AQDFDIVAMS QGKEMIKQRM
     KEIRDKGNDA STKEVNLLTV LELANEMCER GFNFKMVDIE KSDAVNFVIE GDSLIAPFRS
     IPGLGLNVAN KIVEARQEQP FISKKDLATR GKVSKTLIDY MTENKVLDDL PDENQLSLFD
     F
//
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