DPO3B_STAEQ
ID DPO3B_STAEQ Reviewed; 377 AA.
AC Q5HK00;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Beta sliding clamp;
DE Short=Beta clamp;
DE Short=Sliding clamp;
DE AltName: Full=Beta-clamp processivity factor;
DE AltName: Full=DNA polymerase III beta sliding clamp subunit;
DE AltName: Full=DNA polymerase III subunit beta;
GN Name=dnaN; OrderedLocusNames=SERP2552;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
CC -!- FUNCTION: Confers DNA tethering and processivity to DNA polymerases and
CC other proteins. Acts as a clamp, forming a ring around DNA (a reaction
CC catalyzed by the clamp-loading complex) which diffuses in an ATP-
CC independent manner freely and bidirectionally along dsDNA. Initially
CC characterized for its ability to contact the catalytic subunit of DNA
CC polymerase III (Pol III), a complex, multichain enzyme responsible for
CC most of 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:0000250|UniProtKB:P0A988}.
CC -!- SUBUNIT: Forms a ring-shaped head-to-tail homodimer around DNA which
CC binds and tethers DNA polymerases and other proteins to the DNA. The
CC DNA replisome complex has a single clamp-loading complex (3 tau and 1
CC each of delta, delta', psi and chi subunits) which binds 3 Pol III
CC cores (1 core on the leading strand and 2 on the lagging strand) each
CC with a beta sliding clamp dimer. Additional proteins in the replisome
CC are other copies of gamma, psi and chi, Ssb, DNA helicase and RNA
CC primase. {ECO:0000250|UniProtKB:P0A988}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A988}.
CC -!- SIMILARITY: Belongs to the beta sliding clamp family. {ECO:0000305}.
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DR EMBL; CP000029; AAW53376.1; -; Genomic_DNA.
DR RefSeq; WP_001831813.1; NC_002976.3.
DR AlphaFoldDB; Q5HK00; -.
DR SMR; Q5HK00; -.
DR STRING; 176279.SERP2552; -.
DR EnsemblBacteria; AAW53376; AAW53376; SERP2552.
DR GeneID; 50017416; -.
DR KEGG; ser:SERP2552; -.
DR eggNOG; COG0592; Bacteria.
DR HOGENOM; CLU_038149_2_0_9; -.
DR OMA; YLIMPVR; -.
DR OrthoDB; 1040142at2; -.
DR Proteomes; UP000000531; 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-KW.
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; 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;
KW Cytoplasm; DNA replication; DNA-binding; DNA-directed DNA polymerase;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..377
FT /note="Beta sliding clamp"
FT /id="PRO_0000105470"
SQ SEQUENCE 377 AA; 42102 MW; 4188F2AFFD3BCBDD CRC64;
MMEFTIKRDY FINQLNDTLK AISPRTTLPI LTGIKIDAKE NEVILTGSDS EISIEITIPK
QVDGEEIVEI TETGSVVLPG RFFVDIIKKL PGKEVKLSTN EQFQTLITSG HSEFNLSGLD
PDQYPLLPEV SRDDAIQLSV KVLKNIIAQT NFAVSTSETR PVLTGVNWLI QDNELICTAT
DSHRLAVRKL QLEDESENKN VIIPGKALSE LNKIMSDSDE DIDIFFASNQ VLFRVGNINF
ISRLLEGHYP DTTRLFPENY EIKLGINNGD FYHAIDRASL LAREGGNNVI KLSTGNELVE
LSSTSPEIGT VKEEVNANDV EGGNLKISFN SKYMMDALKA IDNDEVEVEF FGTMKPFILK
PKDDDSVTQL ILPIRTY