(data stored in ACNUC7421 zone)
SWISSPROT: Q5LWV3_RUEPO
ID Q5LWV3_RUEPO Unreviewed; 372 AA.
AC Q5LWV3;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 08-MAY-2019, entry version 98.
DE RecName: Full=Beta sliding clamp {ECO:0000256|PIRNR:PIRNR000804};
GN Name=dnaN {ECO:0000313|EMBL:AAV93478.1};
GN OrderedLocusNames=SPO0150 {ECO:0000313|EMBL:AAV93478.1};
OS Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS (Silicibacter pomeroyi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Ruegeria.
OX NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93478.1, ECO:0000313|Proteomes:UP000001023};
RN [1] {ECO:0000313|EMBL:AAV93478.1, ECO:0000313|Proteomes:UP000001023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC {ECO:0000313|Proteomes:UP000001023};
RX PubMed=15602564; DOI=10.1038/nature03170;
RA Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA Haft D.H., Selengut J., Ward N.;
RT "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT marine environment.";
RL Nature 432:910-913(2004).
RN [2] {ECO:0000313|EMBL:AAV93478.1, ECO:0000313|Proteomes:UP000001023}
RP GENOME REANNOTATION.
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC {ECO:0000313|Proteomes:UP000001023};
RX PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA Rivers A.R., Smith C.B., Moran M.A.;
RT "An updated genome annotation for the model marine bacterium Ruegeria
RT pomeroyi DSS-3.";
RL Stand. Genomic Sci. 9:11-11(2014).
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}.
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; CP000031; AAV93478.1; -; Genomic_DNA.
DR RefSeq; WP_011045921.1; NC_003911.12.
DR STRING; 246200.SPO0150; -.
DR EnsemblBacteria; AAV93478; AAV93478; SPO0150.
DR KEGG; sil:SPO0150; -.
DR eggNOG; ENOG4105CZ8; Bacteria.
DR eggNOG; COG0592; LUCA.
DR HOGENOM; HOG000071791; -.
DR KO; K02338; -.
DR OMA; NYEAVIP; -.
DR OrthoDB; 1040142at2; -.
DR BioCyc; RPOM246200:G1G48-154-MONOMER; -.
DR Proteomes; UP000001023; Chromosome.
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; Q5LWV3.
DR SWISS-2DPAGE; Q5LWV3.
KW Complete proteome {ECO:0000313|Proteomes:UP000001023};
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:AAV93478.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001023};
KW Transferase {ECO:0000256|PIRNR:PIRNR000804,
KW ECO:0000256|SAAS:SAAS00729371, ECO:0000313|EMBL:AAV93478.1}.
FT DOMAIN 1 120 DNA_pol3_beta. {ECO:0000259|Pfam:
FT PF00712}.
FT DOMAIN 133 249 DNA_pol3_beta_2. {ECO:0000259|Pfam:
FT PF02767}.
FT DOMAIN 252 371 DNA_pol3_beta_3. {ECO:0000259|Pfam:
FT PF02768}.
SQ SEQUENCE 372 AA; 40383 MW; 26D139C1196AC58D CRC64;
MKISIERGAL LKAVAQAQSV VERRNTIPIL ANVLIEAEGE GAQFRATDLD IEVVDKAPAM
IERAGATTVS ATTLHEIVRK LPDGALVTLT ADAAAGRLTV EAGRSNFSLA TLPREDFPVM
ASSEYQSNFT ANAAVLRRLF DKSKFAISTE ETRYYLNGVY MHVADGDGGK VLRCVATDGH
RLARIDADLP AGATDMPGVI VPRKTVGELR KLLDDDEMDI AVSVSETKVR FATPDITLTS
KVIDGTFPDY TRVIPQANTR RLEVDASEFA KAVDRVATVS SERSRAVKLQ LDEDKLVLSV
NAPDSGAAEE ELAVAYSDER LEIGFNAKYL LEIASQVDRE NAVFLFNSSG DPTLMREGND
QSAVYVVMPM RV
//
If you have problems or comments...
Back to PBIL home page