(data stored in SCRATCH zone)

SWISSPROT: Q3Z4S9_SHISS

ID   Q3Z4S9_SHISS            Unreviewed;       641 AA.
AC   Q3Z4S9;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 100.
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:AAZ87233.1};
GN   OrderedLocusNames=SSON_0457 {ECO:0000313|EMBL:AAZ87233.1};
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269 {ECO:0000313|EMBL:AAZ87233.1, ECO:0000313|Proteomes:UP000002529};
RN   [1] {ECO:0000313|EMBL:AAZ87233.1, ECO:0000313|Proteomes:UP000002529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046 {ECO:0000313|EMBL:AAZ87233.1,
RC   ECO:0000313|Proteomes:UP000002529};
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme
CC       responsible for most of the replicative synthesis in bacteria.
CC       This DNA 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-
CC         COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.7;
CC         Evidence={ECO:0000256|RuleBase:RU364063};
CC   -!- SUBUNIT: DNA polymerase III contains a core (composed of alpha,
CC       epsilon and theta chains) that associates with a tau subunit. This
CC       core dimerizes to form the POLIII' complex. PolIII' associates
CC       with the gamma complex (composed of gamma, delta, delta', psi and
CC       chi chains) and with the beta chain to form the complete DNA
CC       polymerase III complex. {ECO:0000256|RuleBase:RU364063}.
CC   -!- SIMILARITY: Belongs to the DnaX/STICHEL family.
CC       {ECO:0000256|RuleBase:RU364063}.
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DR   EMBL; CP000038; AAZ87233.1; -; Genomic_DNA.
DR   EnsemblBacteria; AAZ87233; AAZ87233; SSON_0457.
DR   KEGG; ssn:SSON_0457; -.
DR   HOGENOM; HOG000083934; -.
DR   KO; K02343; -.
DR   OMA; YALHQGN; -.
DR   BioCyc; SSON300269:G1GL2-526-MONOMER; -.
DR   Proteomes; UP000002529; Chromosome.
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; 3.30.300.150; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR022001; DNA_pol3_tau_IV.
DR   InterPro; IPR022754; DNA_pol_III_gamma-3.
DR   InterPro; IPR012763; DNA_pol_III_sug/sutau.
DR   InterPro; IPR021029; DNA_pol_III_tau_dom-5.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038249; PolIII_tau_C_sf.
DR   Pfam; PF12169; DNA_pol3_gamma3; 1.
DR   Pfam; PF12168; DNA_pol3_tau_4; 1.
DR   Pfam; PF12170; DNA_pol3_tau_5; 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;
DR   PRODOM; Q3Z4S9.
DR   SWISS-2DPAGE; Q3Z4S9.
KW   ATP-binding {ECO:0000256|RuleBase:RU364063};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002529};
KW   DNA replication {ECO:0000256|RuleBase:RU364063};
KW   DNA-directed DNA polymerase {ECO:0000256|RuleBase:RU364063};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU364063};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU364063};
KW   Transferase {ECO:0000256|RuleBase:RU364063}.
FT   DOMAIN       37    178       AAA. {ECO:0000259|SMART:SM00382}.
SQ   SEQUENCE   641 AA;  70867 MW;  0AAC2341D7FB8E88 CRC64;
     MSYQVLARKW RPQTFADVVG QEHVLTALAN GLSLGRIHHA YLFSGTRGVG KTSIARLLAK
     GLNCETGITA TPCGVCDNCR EIEQGRFVDL IEIDAASRTK VEDTRDLLDN VQYAPARGRF
     KVYLIDEVHM LSRHSFNALL KTLEEPPEHV KFLLATTDPQ KLPVTILSRC LQFHLKALDV
     EQIRHQLEHI LNEEHIAHEP RALQLLARAA EGSLRDALSL TDQAIASGDG QVSTQAVSAM
     LGTLDDDQAL SLVEAMVEAN GERVMALINE AAARGIEWEA LLVEMLGLLH RIAMVQLSPA
     ALGNDMAAIE LRMRELARTI PPTDIQLYYQ TLLIGRKELP YAPDRRMGVE MTLLRALAFH
     PRMPLPEPEV PRQSFAPVVP TAVMTPTQVP PQSAPQQAPT VPLPETTSQV LAARQQLQCV
     QGATKAKKSE SAAATRARPV NNAALERLAS VTDRVQARPV PSALEKASAK KEAYRWKATT
     PVMQQKEVVA TPKALKKALE HEKTPELAAK LAAEAIERDP WAAQVSQLSL PKLVEQVALN
     AWKEESDNAV CLHLRSSQRH LNNRGAQQKL AEALSMLKGS TVELTIVEDD NPAVRTPLEW
     RQAIYEEKLA QARESIIADN NIQTLRRFFD AELDEESIRP I
//

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