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Database: UniProt
Entry: A0A1T4XMW3_9CLOT
LinkDB: A0A1T4XMW3_9CLOT
Original site: A0A1T4XMW3_9CLOT 
ID   A0A1T4XMW3_9CLOT        Unreviewed;       543 AA.
AC   A0A1T4XMW3;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
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   ORFNames=SAMN05428976_11528 {ECO:0000313|EMBL:SKA90857.1};
OS   Clostridium sp. USBA 49.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1881060 {ECO:0000313|EMBL:SKA90857.1, ECO:0000313|Proteomes:UP000190748};
RN   [1] {ECO:0000313|EMBL:SKA90857.1, ECO:0000313|Proteomes:UP000190748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USBA 49 {ECO:0000313|EMBL:SKA90857.1,
RC   ECO:0000313|Proteomes:UP000190748};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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|ARBA:ARBA00024632,
CC         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}.
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DR   EMBL; FUYD01000015; SKA90857.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T4XMW3; -.
DR   STRING; 1881060.SAMN05428976_11528; -.
DR   OrthoDB; 9810148at2; -.
DR   Proteomes; UP000190748; Unassembled WGS sequence.
DR   GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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   CDD; cd00009; AAA; 1.
DR   CDD; cd18137; HLD_clamp_pol_III_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; 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; IPR048448; DnaX-like_C.
DR   InterPro; IPR045085; HLD_clamp_pol_III_gamma_tau.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR02397; dnaX_nterm; 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; PF20964; DnaX_C; 1.
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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU364063};
KW   DNA replication {ECO:0000256|RuleBase:RU364063};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|RuleBase:RU364063};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU364063};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU364063};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190748};
KW   Transferase {ECO:0000256|RuleBase:RU364063}.
FT   DOMAIN          37..179
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   543 AA;  62601 MW;  E1A3AF399B8658E3 CRC64;
     MAYTALYREW RPKTFSDVVG QKHITTTLKN QIKNNRIAHA YLLCGTRGTG KTSTAKILAK
     AVNCLNIQDG EPCNECESCK KINAGLSIDF VELDAASYRG IDKIRDIIDE VQYPPRESKY
     KVYIIDEVHM LTKEAVNAFL KTLEEPPSNV IFILATTDPQ MLPITILSRC QRFDFTRIRP
     EDMFERLRKI VKENGVFADD RSLNLIAKMS DGAMRDALSI LDQAISMGNG KVEYDEVVNM
     LGLVTNENLF KLIDAIIERN VEKSMKIVDE VVFSGKDIYN FIKDLIIHLR NLMMVKISKN
     PEDVLDMSYE NIENLKSQAQ KIRIEEIMRD IRILQEAQEQ SKWSKQSRIY LELAVIKLCK
     IEYDTSNEVI LSRLNRLEEN LKNGQISITN KENINAFNNS LKKQSAKTEL KTKNIEKTEI
     KQLDEYNTNS KLNIDIIRKN WRDILEMLKA RNSRANAALL DTGEPVSFKN GIIEVRFDEL
     HAFSKQRLEG EENRKIVEDV FSQALKEKVR IKYTVDKKQN LIKSPEEIIK ETFGEDVVEI
     IDE
//
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