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HOLA_BUCBP
ID   HOLA_BUCBP              Reviewed;         332 AA.
AC   Q89AC0;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2003, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=DNA polymerase III subunit delta;
DE            EC=2.7.7.7;
GN   Name=holA; OrderedLocusNames=bbp_396;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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. The delta
CC       subunit seems to interact with the gamma subunit to transfer the beta
CC       subunit on the DNA (By similarity). {ECO:0000250}.
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   -!- 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 complex
CC       (By similarity). {ECO:0000250}.
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DR   EMBL; AE016826; AAO27108.1; -; Genomic_DNA.
DR   RefSeq; WP_011091509.1; NC_004545.1.
DR   AlphaFoldDB; Q89AC0; -.
DR   SMR; Q89AC0; -.
DR   STRING; 224915.bbp_396; -.
DR   PRIDE; Q89AC0; -.
DR   EnsemblBacteria; AAO27108; AAO27108; bbp_396.
DR   GeneID; 56470933; -.
DR   KEGG; bab:bbp_396; -.
DR   eggNOG; COG1466; Bacteria.
DR   HOGENOM; CLU_044694_0_2_6; -.
DR   OMA; RIPTGKP; -.
DR   OrthoDB; 1199768at2; -.
DR   Proteomes; UP000000601; Chromosome.
DR   GO; GO:0009360; C:DNA polymerase III complex; 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   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR032780; DNA_pol3_delt_C.
DR   InterPro; IPR010372; DNA_pol3_delta_N.
DR   InterPro; IPR005790; DNA_polIII_delta.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF14840; DNA_pol3_delt_C; 1.
DR   Pfam; PF06144; DNA_pol3_delta; 1.
DR   SUPFAM; SSF48019; SSF48019; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01128; holA; 1.
PE   3: Inferred from homology;
KW   DNA replication; DNA-directed DNA polymerase; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN           1..332
FT                   /note="DNA polymerase III subunit delta"
FT                   /id="PRO_0000105504"
SQ   SEQUENCE   332 AA;  39291 MW;  97B14F10E2A67457 CRC64;
     MKIIHSENLF SYSFKTLSSY YVIVGNVKHL IQQSTNIILN LAKKNGFSKM SKIIFCDPIY
     INNIILSAKS QNLFFKKKII SISFKKYISI KEVQNYILKL KKYLHTNLLL IIYIYSTNTN
     ILNKINTKIF PPNGTMITCT FFNQNNISIW TKYKIKNIKM NITKNAENLL IQYHQGNVLH
     LNNTLNILSL VWKNKLINTL SITNFIEDCS IFKPLQWINA LLNNNLQFSI KILNQFENQN
     FNPIILIRYL QHDLLTILLI KRDDVKNYYN ILKNRNTNKN RHSLIINYAR RKHYKTIYKS
     IKLLTLIELQ IKKNNTKLIW LPFYTLSIII CL
 
 
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