(data stored in SCRATCH zone)

SWISSPROT: Q147E9_PARXL

ID   Q147E9_PARXL            Unreviewed;       367 AA.
AC   Q147E9;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 92.
DE   RecName: Full=Beta sliding clamp {ECO:0000256|PIRNR:PIRNR000804};
GN   ORFNames=Bxe_A4461 {ECO:0000313|EMBL:ABE28540.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE28540.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE28540.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE28540.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Confers DNA tethering and processivity to DNA
CC       polymerases and other proteins. Acts as a clamp, forming a ring
CC       around DNA (a reaction catalyzed by the clamp-loading complex)
CC       which diffuses in an ATP-independent manner freely and
CC       bidirectionally along dsDNA. Initially characterized for its
CC       ability to contact the catalytic subunit of DNA polymerase III
CC       (Pol III), a complex, multichain enzyme responsible for most of
CC       the replicative synthesis in bacteria; Pol III exhibits 3'-5'
CC       exonuclease proofreading activity. The beta chain is required for
CC       initiation of replication as well as for processivity of DNA
CC       replication. {ECO:0000256|PIRNR:PIRNR000804}.
CC   -!- SUBUNIT: Forms a ring-shaped head-to-tail homodimer around DNA.
CC       {ECO:0000256|PIRNR:PIRNR000804}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR000804,
CC       ECO:0000256|SAAS:SAAS00729396}.
CC   -!- SIMILARITY: Belongs to the beta sliding clamp family.
CC       {ECO:0000256|PIRNR:PIRNR000804, ECO:0000256|SAAS:SAAS00859809}.
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DR   EMBL; CP000270; ABE28540.1; -; Genomic_DNA.
DR   RefSeq; WP_007180118.1; NZ_CP008760.1.
DR   STRING; 266265.Bxe_A4461; -.
DR   EnsemblBacteria; ABE28540; ABE28540; Bxe_A4461.
DR   GeneID; 4002498; -.
DR   KEGG; bxb:DR64_2133; -.
DR   KEGG; bxe:Bxe_A4461; -.
DR   eggNOG; ENOG4105CZ8; Bacteria.
DR   eggNOG; COG0592; LUCA.
DR   HOGENOM; HOG000071791; -.
DR   KO; K02338; -.
DR   OMA; NYEAVIP; -.
DR   OrthoDB; 1040142at2; -.
DR   BioCyc; BXEN266265:BXE_RS00010-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd00140; beta_clamp; 1.
DR   InterPro; IPR001001; DNA_polIII_beta.
DR   InterPro; IPR022635; DNA_polIII_beta_C.
DR   InterPro; IPR022637; DNA_polIII_beta_cen.
DR   InterPro; IPR022634; DNA_polIII_beta_N.
DR   PANTHER; PTHR30478; PTHR30478; 1.
DR   Pfam; PF00712; DNA_pol3_beta; 1.
DR   Pfam; PF02767; DNA_pol3_beta_2; 1.
DR   Pfam; PF02768; DNA_pol3_beta_3; 1.
DR   PIRSF; PIRSF000804; DNA_pol_III_b; 1.
DR   SMART; SM00480; POL3Bc; 1.
DR   TIGRFAMs; TIGR00663; dnan; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q147E9.
DR   SWISS-2DPAGE; Q147E9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR000804,
KW   ECO:0000256|SAAS:SAAS00729481};
KW   DNA replication {ECO:0000256|PIRNR:PIRNR000804,
KW   ECO:0000256|SAAS:SAAS00729460};
KW   DNA-binding {ECO:0000256|SAAS:SAAS00859811};
KW   DNA-directed DNA polymerase {ECO:0000256|PIRNR:PIRNR000804,
KW   ECO:0000256|SAAS:SAAS00729479};
KW   Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR000804,
KW   ECO:0000256|SAAS:SAAS00729386, ECO:0000313|EMBL:ABE28540.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000804,
KW   ECO:0000256|SAAS:SAAS00729371, ECO:0000313|EMBL:ABE28540.1}.
FT   DOMAIN        6    119       DNA_pol3_beta. {ECO:0000259|Pfam:
FT                                PF00712}.
FT   DOMAIN      131    244       DNA_pol3_beta_2. {ECO:0000259|Pfam:
FT                                PF02767}.
FT   DOMAIN      247    366       DNA_pol3_beta_3. {ECO:0000259|Pfam:
FT                                PF02768}.
SQ   SEQUENCE   367 AA;  40954 MW;  A55B818D80E9B586 CRC64;
     MQLVKTERDN LLRPLQTVSG IVERRHTLPI LANLLITKNG PDVSFLSTDL ELQITTRADF
     GVGGDSVATT VAARKLLDIL RAMPDGQVTL TLNDKRLTVQ SGKSRFALQT LAADEFPTVA
     QAKDYGANLV VPQKTFRQLL GMVHFSMAQQ DIRYYLNGML LVVDGDQLMA VATDGHRLAF
     SSMKIEGSFQ RQEVIIPRKT ILELQRLLED IDDTLKIDIA QTQVKFTFGQ VELVSKLVEG
     KFPDFQRVIP KSHKNQFVIG REELQRSLQR AAILTSDKFK GVRCIIEPGQ LKIMSTNADQ
     EEAQEELEIA YDGDSVDIGF NVTYLLDVLA NLKVDTLQVS LGDASSSALI TIPENDEFKY
     VVMPMRI
//

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