ID   DPO3_UREPA              Reviewed;        1442 AA.
AC   Q9PQB4;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=DNA polymerase III PolC-type {ECO:0000255|HAMAP-Rule:MF_00356};
DE            Short=PolIII {ECO:0000255|HAMAP-Rule:MF_00356};
DE            EC=2.7.7.7 {ECO:0000255|HAMAP-Rule:MF_00356};
GN   Name=polC {ECO:0000255|HAMAP-Rule:MF_00356}; OrderedLocusNames=UU377;
OS   Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX   NCBI_TaxID=273119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700970;
RX   PubMed=11048724; DOI=10.1038/35037619;
RA   Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA   Cassell G.H.;
RT   "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL   Nature 407:757-762(2000).
CC   -!- FUNCTION: Required for replicative DNA synthesis. This DNA polymerase
CC       also exhibits 3' to 5' exonuclease activity. {ECO:0000255|HAMAP-
CC       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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00356};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00356}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-C family. PolC
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00356}.
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DR   EMBL; AF222894; AAF30786.1; -; Genomic_DNA.
DR   RefSeq; WP_010891752.1; NC_002162.1.
DR   AlphaFoldDB; Q9PQB4; -.
DR   SMR; Q9PQB4; -.
DR   STRING; 273119.UU377; -.
DR   PRIDE; Q9PQB4; -.
DR   EnsemblBacteria; AAF30786; AAF30786; UU377.
DR   GeneID; 29672520; -.
DR   KEGG; uur:UU377; -.
DR   PATRIC; fig|273119.6.peg.391; -.
DR   eggNOG; COG2176; Bacteria.
DR   HOGENOM; CLU_003297_1_0_14; -.
DR   OMA; YYAAYFT; -.
DR   Proteomes; UP000000423; 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   Gene3D; 1.10.150.700; -; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   HAMAP; MF_00356; DNApol_PolC; 1.
DR   InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR   InterPro; IPR040982; DNA_pol3_finger.
DR   InterPro; IPR029460; DNAPol_HHH.
DR   InterPro; IPR006054; DnaQ.
DR   InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR   InterPro; IPR004013; PHP_dom.
DR   InterPro; IPR003141; Pol/His_phosphatase_N.
DR   InterPro; IPR016195; Pol/histidinol_Pase-like.
DR   InterPro; IPR006308; PolC_gram_pos.
DR   InterPro; IPR044923; PolC_middle_finger_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
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   SMART; SM00479; EXOIII; 1.
DR   SMART; SM00481; POLIIIAc; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF89550; SSF89550; 1.
DR   TIGRFAMs; TIGR00573; dnaq; 1.
DR   TIGRFAMs; TIGR01405; polC_Gram_pos; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA replication; DNA-directed DNA polymerase; Exonuclease;
KW   Hydrolase; Nuclease; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..1442
FT                   /note="DNA polymerase III PolC-type"
FT                   /id="PRO_0000204607"
FT   DOMAIN          409..568
FT                   /note="Exonuclease"
SQ   SEQUENCE   1442 AA;  166229 MW;  834C3EF722ACA6D1 CRC64;
     METKNALFKK IVKISDQLLN KISIKKLTKD KKNNLFVYFD EFVDVTIIDE LHQLSKTTLM
     HDLQIWYINN LKEVDHKKIL TFFKKISEQN ANLIFLEQIN DLNTKIEYNS NLNSLILKIN
     DKLIYDHFIA NKLEILNILK VWSLPYSNFE IHFENLSSLL NEKHEQAVNE IISHHIQQQK
     HLEQQISQQQ NFYNNQKANF NYYKNPSNKT ITKLIDINPL MNNAKIRAYV FLKKIDILKS
     GAIAYKLNVI DDSETLTIMT YLPSGEHPLK KFLDELKIDQ LIEAEIDIVL DNMSKSGQVP
     IGKIKKICCV EDKHVKKQIT PRLELNFHTK MSSLDAIIST QELIDFAVKN QLKTIGITDR
     NVVQAYPEIA KFSKKQDLKI IYGLETEELE DQIPLVLNVR DQNLDNATYV IFDIETTGLF
     PNFDEIIEFG AVIMQNNKQI GEKIQFFIKP IQQINENVTN LTNISQEMVN NAIDEKTALL
     KIKEIFDDHI LVAHNGINFD INFINQRLLK WGLEPLKNPS IDTLMISRAI NPFKSHRLGA
     ICKKYEVDYN DESAHRADYD AIVLADVFKV MKNNLFNDFG ITNLSEINTK LQTTMLKNRS
     FGNWINLYIK NQANVKDMYE LVSISHTDMY YTRPTITTSF LANKKDKLII SNSIHESDLI
     NALYSKNDEE IKRLIQRYDF ITLPSLGSQK HLVYAKKITI ENVQKAFKKL IYLALELNKI
     IIYSSSPYYF FKDDKKFYDV YVNTKGLEGK AHRFANEVYV PDLEYIDQKN AIDELAYLED
     EKLINLIINE NPVHINSWFD DSIQPLKEGL YAPKMEGVDQ KTIDYVYHTA KKIYGENLPT
     IVEQRIKKEL NSIIKHGFSV VYWISHLLVE KSMQDGYGVG SRGSVGSSLV ATFLNITDVN
     PLTPHYLCPN CKKCEFITNA DDGFDLAPKS CEQCQTPMLT DGHNIPFETF LGFDGDKVPD
     IDLNFSGVYQ AVAHNFIKSI FGETHSYRAG TIGTMAQTSA ENTVKKYFEN RFNENKIIRD
     STVSLYVQKC IDSKRTTGQH PGGIIIVPKE YSIWDFSPYN FPANDINETW KTTHFAFEYL
     HDSLLKFDIL GHDNPTILKL LKDYTGIDER DVPMYDPLVM KSFSDISALN IKPSDVLNET
     TGAISIPEFG TRFVRGMLVD TKPKSFADLI RISGLSHGES VWLGNAQSLI KSGKLLKDVI
     ACRDDIMTYL IRQNVEPKTA FLIMEDVRKG KKIKPEHQII LKELKVPEWY IESANKIKYM
     FPKAHATAYV MHAWKFAWYK IYYPLEYYAA FFSVRADNFD LFVINQGKEF IEKTYNDIEQ
     RSKSRDPQKK VSSRELALQP IYEIVIELLA RGFKISNISI EQSQATSYVI DKENNAIIPP
     FIAIQGLGET VANSIIEARN QKVFSTIEDL KNRTKISRTD LKNLRVLGVL DHLSETEQLT
     LF