ID   DPO3X_BACSU             Reviewed;         563 AA.
AC   P09122;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 3.
DT   02-SEP-2026, entry version 157.
DE   RecName: Full=DNA polymerase III subunit tau;
DE            EC=2.7.7.7;
GN   Name=dnaX {ECO:0000303|PubMed:2468993, ECO:0000303|PubMed:9384377};
GN   Synonyms=dnaH {ECO:0000303|PubMed:7584024}, dnaZX
GN   {ECO:0000303|PubMed:2452406}; OrderedLocusNames=BSU00190;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / YB886 / BG214;
RX   PubMed=2124672; DOI=10.1093/nar/18.23.6771;
RA   Alonso J.C., Shirahige K., Ogasawara N.;
RT   "Molecular cloning, genetic characterization and DNA sequence analysis of
RT   the recM region of Bacillus subtilis.";
RL   Nucleic Acids Res. 18:6771-6777(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   SEQUENCE REVISION TO 211 AND 533.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-422.
RC   STRAIN=168;
RX   PubMed=2452406; DOI=10.1093/nar/16.6.2720;
RA   Struck J.C.R., Vogel D.W., Ulbrich N., Erdmann V.A.;
RT   "A dnaZX-like open reading frame downstream from the Bacillus subtilis
RT   scRNA gene.";
RL   Nucleic Acids Res. 16:2720-2720(1988).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5.
RC   STRAIN=168;
RX   PubMed=2468993; DOI=10.1007/bf00427046;
RA   Struck J.C.R., Hartmann R.K., Toschka H.Y., Erdmann V.A.;
RT   "Transcription and processing of Bacillus subtilis small cytoplasmic RNA.";
RL   Mol. Gen. Genet. 215:478-482(1989).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5.
RC   STRAIN=168;
RX   PubMed=1698458; DOI=10.1016/0167-4781(90)90145-r;
RA   Struck J.C.R., Kretschmer-Kazemi F.R., Schroeder W., Hucho F.,
RA   Toschka H.Y., Erdmann V.A.;
RT   "Characterization of a 17 kDa protein gene upstream from the small
RT   cytoplasmic RNA gene of Bacillus subtilis.";
RL   Biochim. Biophys. Acta 1050:80-83(1990).
RN   [8]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=168;
RX   PubMed=17853894; DOI=10.1038/sj.emboj.7601848;
RA   Lecointe F., Serena C., Velten M., Costes A., McGovern S., Meile J.C.,
RA   Errington J., Ehrlich S.D., Noirot P., Polard P.;
RT   "Anticipating chromosomal replication fork arrest: SSB targets repair DNA
RT   helicases to active forks.";
RL   EMBO J. 26:4239-4251(2007).
RN   [9]
RP   SUBUNIT.
RX   PubMed=23525462; DOI=10.1093/nar/gkt173;
RA   Afonso J.P., Chintakayala K., Suwannachart C., Sedelnikova S., Giles K.,
RA   Hoyes J.B., Soultanas P., Rafferty J.B., Oldham N.J.;
RT   "Insights into the structure and assembly of the Bacillus subtilis clamp-
RT   loader complex and its interaction with the replicative helicase.";
RL   Nucleic Acids Res. 41:5115-5126(2013).
CC   -!- FUNCTION: Part of the beta sliding clamp loading complex, which
CC       hydrolyzes ATP to load the beta clamp onto primed DNA to form the DNA
CC       replication pre-initiation complex. DNA polymerase III is a complex,
CC       multichain enzyme responsible for most of the replicative DNA synthesis
CC       in bacteria. {ECO:0000250|UniProtKB:P06710}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) +
CC         diphosphate; Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-
CC         COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112;
CC         EC=2.7.7.7;
CC   -!- SUBUNIT: Component of the DNA clamp loading complex consisting of
CC       tau(3):delta(1):delta'(1) (PubMed:23525462). The DNA polymerase III
CC       holoenzyme complex contains at least 10 different subunits organized
CC       into 3 functionally essential subassemblies: the Pol III core, the beta
CC       sliding clamp processivity factor and the clamp-loading complex. The
CC       Pol III core (subunits alpha, epsilon and theta) contains the
CC       polymerase and the 3'-5' exonuclease proofreading activities. The
CC       polymerase is tethered to the template via the dimeric beta sliding
CC       clamp processivity factor. The DNA clamp-loading complex assembles the
CC       beta sliding clamp onto the primed template and plays a central role in
CC       the organization and communication at the replication fork (By
CC       similarity). Forms a complex with replicative DNA helicase DnaB (shown
CC       with G.stearothermophilus DnaB) tau(3):DnaB(6); a single ATP hydrolysis
CC       even is sufficient for complex formation (PubMed:23525462). Colocalizes
CC       with DNA helicases PriA, RecQ and RecS (PubMed:17853894).
CC       {ECO:0000250|UniProtKB:P06710, ECO:0000269|PubMed:17853894,
CC       ECO:0000269|PubMed:23525462}.
CC   -!- INTERACTION:
CC       P09122; Q9X4C9: dnaB; Xeno; NbExp=2; IntAct=EBI-5243974, EBI-6402993;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid
CC       {ECO:0000269|PubMed:17853894}. Note=Localizes in tight foci to the
CC       chromosomal replication center at mid-cell; positioning does not rely
CC       on the C-terminus of SSB (ssbA) (PubMed:17853894).
CC       {ECO:0000269|PubMed:17853894}.
CC   -!- MISCELLANEOUS: Unlike E.coli this gene does not also produce the
CC       shortened gamma protein; there is no defined order for DNA clamp
CC       loading complex assembly (PubMed:23525462).
CC       {ECO:0000269|PubMed:23525462}.
CC   -!- SIMILARITY: Belongs to the DnaX/STICHEL family. {ECO:0000305}.
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DR   EMBL; X17014; CAA34877.1; -; Genomic_DNA.
DR   EMBL; D26185; BAA05255.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11795.2; -; Genomic_DNA.
DR   EMBL; X06803; CAA29958.1; -; Genomic_DNA.
DR   EMBL; X52144; CAA36390.1; -; Genomic_DNA.
DR   PIR; I40469; I40469.
DR   PIR; S13786; S13786.
DR   RefSeq; NP_387900.2; NC_000964.3.
DR   RefSeq; WP_003247135.1; NC_000964.3.
DR   AlphaFoldDB; P09122; -.
DR   SMR; P09122; -.
DR   FunCoup; P09122; 313.
DR   IntAct; P09122; 6.
DR   STRING; 224308.BSU00190; -.
DR   PaxDb; 224308-BSU00190; -.
DR   EnsemblBacteria; CAB11795; CAB11795; BSU_00190.
DR   GeneID; 936899; -.
DR   KEGG; bsu:BSU00190; -.
DR   PATRIC; fig|224308.179.peg.19; -.
DR   eggNOG; COG2812; Bacteria.
DR   InParanoid; P09122; -.
DR   OrthoDB; 9810148at2; -.
DR   PhylomeDB; P09122; -.
DR   BioCyc; BSUB:BSU00190-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro.
DR   GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd18137; HLD_clamp_pol_III_gamma_tau; 1.
DR   FunFam; 1.10.8.60:FF:000013; DNA polymerase III subunit gamma/tau; 1.
DR   FunFam; 1.20.272.10:FF:000003; DNA polymerase III subunit gamma/tau; 1.
DR   FunFam; 3.40.50.300:FF:000014; DNA polymerase III subunit gamma/tau; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.20.272.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR022754; DNA_pol_III_gamma-3.
DR   InterPro; IPR012763; DNA_pol_III_sug/sutau_N.
DR   InterPro; IPR050238; DNA_Rep/Repair_Clamp_Loader.
DR   InterPro; IPR045085; HLD_clamp_pol_III_gamma_tau.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR02397; dnaX_nterm; 1.
DR   NCBIfam; NF004046; PRK05563.1; 1.
DR   PANTHER; PTHR11669:SF0; PROTEIN STICHEL-LIKE 2; 1.
DR   PANTHER; PTHR11669; REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT; 1.
DR   Pfam; PF13177; DNA_pol3_delta2; 1.
DR   Pfam; PF12169; DNA_pol3_gamma3; 1.
DR   Pfam; PF22608; DNAX_ATPase_lid; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; DNA replication; DNA-directed DNA polymerase;
KW   Metal-binding; Nucleotide-binding; Nucleotidyltransferase;
KW   Reference proteome; Transferase; Zinc.
FT   CHAIN           1..563
FT                   /note="DNA polymerase III subunit tau"
FT                   /id="PRO_0000105492"
FT   BINDING         45..52
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         64
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P06710"
FT   BINDING         73
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P06710"
FT   BINDING         76
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P06710"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P06710"
FT   CONFLICT        533
FT                   /note="E -> A (in Ref. 1; CAA34877 and 2; BAA05255)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   563 AA;  62763 MW;  F5975C246622E4F5 CRC64;
     MSYQALYRVF RPQRFEDVVG QEHITKTLQN ALLQKKFSHA YLFSGPRGTG KTSAAKIFAK
     AVNCEHAPVD EPCNECAACK GITNGSISDV IEIDAASNNG VDEIRDIRDK VKFAPSAVTY
     KVYIIDEVHM LSIGAFNALL KTLEEPPEHC IFILATTEPH KIPLTIISRC QRFDFKRITS
     QAIVGRMNKI VDAEQLQVEE GSLEIIASAA DGGMRDALSL LDQAISFSGD ILKVEDALLI
     TGAVSQLYIG KLAKSLHDKN VSDALETLNE LLQQGKDPAK LIEDMIFYFR DMLLYKTAPG
     LEGVLEKVKV DETFRELSEQ IPAQALYEMI DILNKSHQEM KWTNHPRIFF EVAVVKICQT
     SHQSAADLPE VDMLMKKIQQ LEQEVERLKT TGIKAAAESP KKEAPRVPKG GKSNYKAPVG
     RIHEILKEAT RPDLDLLRNS WGKLLAHLKQ QNKVSHAALL NDSEPVAAGS AAFVLKFKYE
     IHCKMVAEDN NGVRTNLEQI LESMLGKRMD LIGVPEAQWG KIREEFLEDH QQENEGSNEP
     AEEDPLIAEA KKLVGADLIE IKD
//