DPO3B_MYCLE
ID DPO3B_MYCLE Reviewed; 399 AA.
AC P46387;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 115.
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=ML0002;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8969512; DOI=10.1099/13500872-142-11-3147;
RA Fsihi H., de Rossi E., Salazar L., Cantoni R., Labo M., Riccardi G.,
RA Takiff H.E., Eiglmeier K., Bergh S., Cole S.T.;
RT "Gene arrangement and organization in an approximately 76 kb fragment
RT encompassing the oriC region of the chromosome of Mycobacterium leprae.";
RL Microbiology 142:3147-3161(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8733228; DOI=10.1111/j.1365-2958.1996.tb02617.x;
RA Salazar L., Fsihi H., De Rossi E., Riccardi G., Rios C., Cole S.T.,
RA Takiff H.E.;
RT "Organization of the origins of replication of the chromosomes of
RT Mycobacterium smegmatis, Mycobacterium leprae and Mycobacterium
RT tuberculosis and isolation of a functional origin from M. smegmatis.";
RL Mol. Microbiol. 20:283-293(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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; L39923; AAB53142.1; -; Genomic_DNA.
DR EMBL; Z70722; CAA94709.1; -; Genomic_DNA.
DR EMBL; AL583917; CAC29510.1; -; Genomic_DNA.
DR PIR; T10002; T10002.
DR RefSeq; NP_301130.1; NC_002677.1.
DR RefSeq; WP_010907455.1; NC_002677.1.
DR AlphaFoldDB; P46387; -.
DR SMR; P46387; -.
DR STRING; 272631.ML0002; -.
DR EnsemblBacteria; CAC29510; CAC29510; CAC29510.
DR KEGG; mle:ML0002; -.
DR PATRIC; fig|272631.5.peg.2; -.
DR Leproma; ML0002; -.
DR eggNOG; COG0592; Bacteria.
DR HOGENOM; CLU_038149_1_1_11; -.
DR OMA; YLIMPVR; -.
DR Proteomes; UP000000806; 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..399
FT /note="Beta sliding clamp"
FT /id="PRO_0000105448"
SQ SEQUENCE 399 AA; 41942 MW; 48680894EBCB9837 CRC64;
MDLAKTNVGC SDLKFCLARE SFASAVSWVA KYLPTRPTVP VLSGVLLTGS DSGLTISGFD
YEVSAEVQVA AEIASSGSVL VSGRLLSDIT RALPNKPVHF YVDGNRVALT CGSARFSLPT
MAVEDYPTLP TLPDETGTLP SDVFAEAIGQ VAIAAGRDYT LPMLTGIRIE ISGDTVVLAA
TDRFRLAVRE LKWSVLSSDF EASVLVPAKT LVEVAKAGTD GSGVCLSLGA GVGVGKDGLF
GISGGGKRST TRLLDAEFPK FRQLLPAEHT AVATIDVAEL TEAIKLVALV ADRGAQVRME
FGDGILRLSA GADDVGRAEE DLAVAFTGEP LTIAFNPNYL TDGLASVHSE RVSFGFTTPS
KPALLRPTSN DDVHPTHDGP FPALPTDYVY LLMPVRLPG
