(data stored in ACNUC7421 zone)

SWISSPROT: DPO3B_BACSU

ID   DPO3B_BACSU             Reviewed;         378 AA.
AC   P05649; P11571;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   11-DEC-2019, entry version 135.
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; Synonyms=dnaG; OrderedLocusNames=BSU00020;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2987847; DOI=10.1093/nar/13.7.2251;
RA   Moriya S., Ogasawara N., Yoshikawa H.;
RT   "Structure and function of the region of the replication origin of the
RT   Bacillus subtilis chromosome. III. Nucleotide sequence of some 10,000 base
RT   pairs in the origin region.";
RL   Nucleic Acids Res. 13:2251-2265(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
RC   STRAIN=168 / PSL1;
RX   PubMed=2846289; DOI=10.1002/j.1460-2075.1988.tb03149.x;
RA   Moriya S., Fukuoka T., Ogasawara N., Yoshikawa H.;
RT   "Regulation of initiation of the chromosomal replication by DnaA-boxes in
RT   the origin region of the Bacillus subtilis chromosome.";
RL   EMBO J. 7:2911-2917(1988).
RN   [5] {ECO:0000244|PDB:4TR6}
RP   X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS), AND SUBUNIT.
RX   PubMed=25170813; DOI=10.1021/jm500467a;
RA   Wolff P., Amal I., Olieric V., Chaloin O., Gygli G., Ennifar E., Lorber B.,
RA   Guichard G., Wagner J., Dejaegere A., Burnouf D.Y.;
RT   "Differential modes of peptide binding onto replicative sliding clamps from
RT   various bacterial origins.";
RL   J. Med. Chem. 57:7565-7576(2014).
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 (PubMed:25170813)
CC       around DNA which binds and tethers DNA polymerases and other proteins
CC       to the DNA. The DNA replisome complex has a single clamp-loading
CC       complex (3 tau and 1 each of delta, delta', psi and chi subunits) which
CC       binds 3 Pol III cores (1 core on the leading strand and 2 on the
CC       lagging strand) each with a beta sliding clamp dimer. Additional
CC       proteins in the replisome are other copies of gamma, psi and chi, Ssb,
CC       DNA helicase and RNA primase. {ECO:0000250|UniProtKB:P0A988,
CC       ECO:0000269|PubMed:25170813}.
CC   -!- INTERACTION:
CC       P37542:yabA; NbExp=4; IntAct=EBI-5244587, EBI-5243764;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A988}.
CC   -!- SIMILARITY: Belongs to the beta sliding clamp family. {ECO:0000305}.
DR   EMBL; X02369; CAA26218.1; -; Genomic_DNA.
DR   EMBL; D26185; BAA05238.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11778.1; -; Genomic_DNA.
DR   EMBL; X12779; CAA31271.1; -; Genomic_DNA.
DR   PIR; B22930; B22930.
DR   RefSeq; NP_387883.1; NC_000964.3.
DR   RefSeq; WP_003242509.1; NZ_JNCM01000034.1.
DR   PDB; 4TR6; X-ray; 1.50 A; A/B=1-378.
DR   PDB; 6E8D; X-ray; 2.34 A; A/B/C/D=1-378.
DR   PDBsum; 4TR6; -.
DR   PDBsum; 6E8D; -.
DR   SMR; P05649; -.
DR   DIP; DIP-61105N; -.
DR   IntAct; P05649; 6.
DR   MINT; P05649; -.
DR   STRING; 224308.BSU00020; -.
DR   jPOST; P05649; -.
DR   PaxDb; P05649; -.
DR   PRIDE; P05649; -.
DR   EnsemblBacteria; CAB11778; CAB11778; BSU00020.
DR   GeneID; 939970; -.
DR   KEGG; bsu:BSU00020; -.
DR   PATRIC; fig|224308.179.peg.2; -.
DR   eggNOG; ENOG4105CZ8; Bacteria.
DR   eggNOG; COG0592; LUCA.
DR   HOGENOM; HOG000071792; -.
DR   InParanoid; P05649; -.
DR   KO; K02338; -.
DR   OMA; YLIMPVR; -.
DR   PhylomeDB; P05649; -.
DR   BioCyc; BSUB:BSU00020-MONOMER; -.
DR   Proteomes; UP000001570; 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:0006271; P:DNA strand elongation involved in DNA replication; IBA:GO_Central.
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   1: Evidence at protein level;
DR   PRODOM; P05649.
DR   SWISS-2DPAGE; P05649.
KW   3D-structure; Cytoplasm; DNA replication; DNA-binding;
KW   DNA-directed DNA polymerase; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..378
FT                   /note="Beta sliding clamp"
FT                   /id="PRO_0000105424"
FT   STRAND          2..6
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   HELIX           7..18
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   HELIX           28..31
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   STRAND          32..37
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   STRAND          39..47
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   STRAND          49..61
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   STRAND          67..71
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   STRAND          73..78
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   HELIX           79..87
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   STRAND          90..98
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   HELIX           100..102
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   STRAND          103..108
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   STRAND          111..116
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   HELIX           120..122
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   STRAND          135..138
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   HELIX           139..147
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   HELIX           150..152
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   STRAND          157..159
FT                   /evidence="ECO:0000244|PDB:6E8D"
FT   HELIX           160..163
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   STRAND          164..170
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   STRAND          173..179
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   STRAND          181..190
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   STRAND          199..204
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   HELIX           205..214
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   STRAND          221..226
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   STRAND          228..235
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   STRAND          238..243
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   TURN            253..255
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   STRAND          261..267
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   HELIX           268..278
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   TURN            279..281
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   STRAND          290..295
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   TURN            296..298
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   STRAND          299..306
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   TURN            307..309
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   STRAND          310..317
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   STRAND          319..324
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   STRAND          326..330
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   HELIX           332..341
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   STRAND          344..352
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   TURN            353..355
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   STRAND          358..361
FT                   /evidence="ECO:0000244|PDB:4TR6"
FT   STRAND          367..372
FT                   /evidence="ECO:0000244|PDB:4TR6"
SQ   SEQUENCE   378 AA;  42103 MW;  C1F040B5D53026C8 CRC64;
     MKFTIQKDRL VESVQDVLKA VSSRTTIPIL TGIKIVASDD GVSFTGSDSD ISIESFIPKE
     EGDKEIVTIE QPGSIVLQAR FFSEIVKKLP MATVEIEVQN QYLTIIRSGK AEFNLNGLDA
     DEYPHLPQIE EHHAIQIPTD LLKNLIRQTV FAVSTSETRP ILTGVNWKVE QSELLCTATD
     SHRLALRKAK LDIPEDRSYN VVIPGKSLTE LSKILDDNQE LVDIVITETQ VLFKAKNVLF
     FSRLLDGNYP DTTSLIPQDS KTEIIVNTKE FLQAIDRASL LAREGRNNVV KLSAKPAESI
     EISSNSPEIG KVVEAIVADQ IEGEELNISF SPKYMLDALK VLEGAEIRVS FTGAMRPFLI
     RTPNDETIVQ LILPVRTY
//

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