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 03-AUG-2022, entry version 145.
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:0007744|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 P05649; 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}.
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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 AlphaFoldDB; P05649; -.
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; BSU_00020.
DR GeneID; 939970; -.
DR KEGG; bsu:BSU00020; -.
DR PATRIC; fig|224308.179.peg.2; -.
DR eggNOG; COG0592; Bacteria.
DR InParanoid; P05649; -.
DR OMA; YLIMPVR; -.
DR PhylomeDB; P05649; -.
DR BioCyc; BSUB:BSU00020-MON; -.
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;
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:0007829|PDB:4TR6"
FT HELIX 7..18
FT /evidence="ECO:0007829|PDB:4TR6"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:4TR6"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:4TR6"
FT STRAND 39..47
FT /evidence="ECO:0007829|PDB:4TR6"
FT STRAND 49..61
FT /evidence="ECO:0007829|PDB:4TR6"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:4TR6"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:4TR6"
FT HELIX 79..87
FT /evidence="ECO:0007829|PDB:4TR6"
FT STRAND 90..98
FT /evidence="ECO:0007829|PDB:4TR6"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:4TR6"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:4TR6"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:4TR6"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:4TR6"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:4TR6"
FT HELIX 139..147
FT /evidence="ECO:0007829|PDB:4TR6"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:4TR6"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:6E8D"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:4TR6"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:4TR6"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:4TR6"
FT STRAND 181..190
FT /evidence="ECO:0007829|PDB:4TR6"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:4TR6"
FT HELIX 205..214
FT /evidence="ECO:0007829|PDB:4TR6"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:4TR6"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:4TR6"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:4TR6"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:4TR6"
FT STRAND 261..267
FT /evidence="ECO:0007829|PDB:4TR6"
FT HELIX 268..278
FT /evidence="ECO:0007829|PDB:4TR6"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:4TR6"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:4TR6"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:4TR6"
FT STRAND 299..306
FT /evidence="ECO:0007829|PDB:4TR6"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:4TR6"
FT STRAND 310..317
FT /evidence="ECO:0007829|PDB:4TR6"
FT STRAND 319..324
FT /evidence="ECO:0007829|PDB:4TR6"
FT STRAND 326..330
FT /evidence="ECO:0007829|PDB:4TR6"
FT HELIX 332..341
FT /evidence="ECO:0007829|PDB:4TR6"
FT STRAND 344..352
FT /evidence="ECO:0007829|PDB:4TR6"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:4TR6"
FT STRAND 358..361
FT /evidence="ECO:0007829|PDB:4TR6"
FT STRAND 367..372
FT /evidence="ECO:0007829|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