ID   A0A6A2FJH1_9BACL        Unreviewed;       558 AA.
AC   A0A6A2FJH1;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   29-SEP-2021, entry version 4.
DE   RecName: Full=DNA polymerase III subunit gamma/tau {ECO:0000256|RuleBase:RU364063};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU364063};
GN   Name=dnaX {ECO:0000256|RuleBase:RU364063,
GN   ECO:0000313|EMBL:KAB2864411.1};
GN   ORFNames=F9K39_05145 {ECO:0000313|EMBL:KAB2864411.1};
OS   Exiguobacterium chiriqhucha.
OC   Bacteria; Firmicutes; Bacilli; Bacillales;
OC   Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX   NCBI_TaxID=1385984 {ECO:0000313|EMBL:KAB2864411.1};
RN   [1] {ECO:0000313|EMBL:KAB2864411.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SB27 {ECO:0000313|EMBL:KAB2864411.1};
RA   Berger S., Rangel Shaw D., Berben T., In 'T Zandt M., Frank J., Reimann J.,
RA   Jetten M.S.M., Welte C.U.;
RT   "Extracellular Electron Transfer in a Candidatus Methanoperedens spp.
RT   Enrichment Culture.";
RL   Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases.
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.
CC       {ECO:0000256|RuleBase:RU364063}.
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|RuleBase:RU364063};
CC   -!- SUBUNIT: DNA polymerase III contains a core (composed of alpha, epsilon
CC       and theta chains) that associates with a tau subunit. This core
CC       dimerizes to form the POLIII' complex. PolIII' associates with the
CC       gamma complex (composed of gamma, delta, delta', psi and chi chains)
CC       and with the beta chain to form the complete DNA polymerase III
CC       complex. {ECO:0000256|RuleBase:RU364063}.
CC   -!- SIMILARITY: Belongs to the DnaX/STICHEL family.
CC       {ECO:0000256|ARBA:ARBA00006360, ECO:0000256|RuleBase:RU364063}.
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:KAB2864411.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; WBUX01000096; KAB2864411.1; -; Genomic_DNA.
DR   GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 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.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF12169; DNA_pol3_gamma3; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF48019; SSF48019; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR02397; dnaX_nterm; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU364063};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA replication {ECO:0000256|RuleBase:RU364063};
KW   DNA-directed DNA polymerase {ECO:0000256|RuleBase:RU364063};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU364063};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU364063,
KW   ECO:0000313|EMBL:KAB2864411.1};
KW   Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:KAB2864411.1}.
FT   DOMAIN          37..183
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   COILED          361..388
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          412..432
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   558 AA;  63577 MW;  98FDE0DD4CB7088F CRC64;
     MAYQALYRVY RPQSFQEVVG QIHITRTIQN ALLEERMSHA YLFSGPRGTG KTSLAKIIAK
     AINCETAPTR EPCNTCPTCI AITEGTSPDV FEIDAASNNG VDEIREIRDK VKYPPSQARF
     KVYIIDEVHM LSTGAFNALL KTLEEPPAHA IFILATTEPH KIPATIISRC QRFDVKRHEV
     GQLQTRMAYI LNDQDYDYDP EALKLIARAA DGGMRDALSL LDQALAFSDG RLTEDAVLEV
     TGAVTDDALL DMAYGLQQKQ LDQILSTLET MLREGKDLKR FIEDLVFVHR DALLLKASPQ
     AVDLLERARP TETFRQFVEA TSTDELFQVI EELNDCQQQM RLSNHPKVLV ELTFIRIAEQ
     GRTMTEQMKQ LQEQVRELSR ELNEVKKTGV PAAEATAEKP KVAKRTQIRV PKERIRQLLQ
     RAERQHLNAI RDSWEDIMGN IRTQDGPIFA LFYESEAVLC ASDTLLVQFK DGMTWHYEQV
     SSNGRTRDVI EQALFEVTGI RREIMAVLET DWVELKNEFI LRKQAERSDH KEEEVDEEDP
     LVSKALERFG DVVEIEEV
//