DPO3B_CAUVN
ID DPO3B_CAUVN Reviewed; 372 AA.
AC B8GXP6; P48198; Q45999;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=CCNA_00155;
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=NA1000 / CB15N;
RX PubMed=9079919; DOI=10.1128/jb.179.7.2319-2330.1997;
RA Roberts R.C., Shapiro L.;
RT "Transcription of genes encoding DNA replication proteins is coincident
RT with cell cycle control of DNA replication in Caulobacter crescentus.";
RL J. Bacteriol. 179:2319-2330(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 199-294.
RX PubMed=8226640; DOI=10.1128/jb.175.21.6970-6981.1993;
RA Rizzo M.F., Shapiro L., Gober J.;
RT "Asymmetric expression of the gyrase B gene from the replication-competent
RT chromosome in the Caulobacter crescentus predivisional cell.";
RL J. Bacteriol. 175:6970-6981(1993).
RN [4]
RP FUNCTION, INTERACTION WITH SOCB AND HDAA, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF GLY-179.
RX PubMed=24239291; DOI=10.1016/j.molcel.2013.10.014;
RA Aakre C.D., Phung T.N., Huang D., Laub M.T.;
RT "A bacterial toxin inhibits DNA replication elongation through a direct
RT interaction with the beta sliding clamp.";
RL Mol. Cell 52:617-628(2013).
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 (By similarity). Interaction with toxin SocB via the
CC hydrophobic cleft blocks DNA replication elongation (PubMed:24239291).
CC {ECO:0000250|UniProtKB:P0A988, ECO:0000269|PubMed:24239291}.
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 (By similarity). Interacts with DNA replication inhibitor toxin
CC SocB (PubMed:24239291). {ECO:0000250|UniProtKB:P0A988,
CC ECO:0000269|PubMed:24239291}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:24239291}.
CC Note=Forms a discrete locus during DNA replication that moves from one
CC pole to mid-cell before dispersing once DNA has been replicated.
CC Overexpressed tagged toxin SocB colocalizes with these loci but causes
CC their premature collapse (PubMed:24239291).
CC {ECO:0000269|PubMed:24239291}.
CC -!- INDUCTION: Has 3 promoters, 1 is heat inducible at 42 degrees Celsius
CC (probably under control of sigma-32). Transcription from the other 2
CC promoters is induced just prior to the onset of DNA replication, at the
CC swarmer-to-stalked-cell transition, lasts through the stalked-cell
CC phase and then decreases in the predivisional cell.
CC {ECO:0000269|PubMed:9079919}.
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted.
CC {ECO:0000269|PubMed:9079919}.
CC -!- SIMILARITY: Belongs to the beta sliding clamp family. {ECO:0000305}.
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DR EMBL; U37793; AAB51448.1; -; Genomic_DNA.
DR EMBL; CP001340; ACL93622.1; -; Genomic_DNA.
DR EMBL; U00591; AAC43045.1; -; Genomic_DNA.
DR PIR; A49347; A49347.
DR RefSeq; WP_010918045.1; NC_011916.1.
DR RefSeq; YP_002515530.1; NC_011916.1.
DR AlphaFoldDB; B8GXP6; -.
DR SMR; B8GXP6; -.
DR PRIDE; B8GXP6; -.
DR EnsemblBacteria; ACL93622; ACL93622; CCNA_00155.
DR GeneID; 7332409; -.
DR KEGG; ccs:CCNA_00155; -.
DR PATRIC; fig|565050.3.peg.153; -.
DR HOGENOM; CLU_038149_4_2_5; -.
DR OMA; YLIMPVR; -.
DR OrthoDB; 1040142at2; -.
DR PhylomeDB; B8GXP6; -.
DR PRO; PR:B8GXP6; -.
DR Proteomes; UP000001364; 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 1: Evidence at protein level;
KW Cytoplasm; DNA replication; DNA-binding; DNA-directed DNA polymerase;
KW Nucleotidyltransferase; Reference proteome; Stress response; Transferase.
FT CHAIN 1..372
FT /note="Beta sliding clamp"
FT /id="PRO_0000378285"
FT MUTAGEN 179
FT /note="G->C: Suppresses growth defects of strains
FT overexpressing SocB, no longer interacts with SocB, still
FT interacts with HdaA. Replication forks do not collapse."
FT /evidence="ECO:0000269|PubMed:24239291"
FT MUTAGEN 179
FT /note="G->R: Suppresses growth defects of strains
FT overexpressing SocB, no longer interacts with SocB or HdaA,
FT cells are filamentous."
FT /evidence="ECO:0000269|PubMed:24239291"
FT CONFLICT 278
FT /note="T -> N (in Ref. 3; AAC43045)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="G -> D (in Ref. 3; AAC43045)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 372 AA; 40425 MW; B4B234778AD89BE4 CRC64;
MKLTIERAAL LKALGHVQSV VERRNTIPIL SNILLSAEGD RLSFSATDLD MEIIDEGFAQ
IDVPGQITAP AHTLYEIVRK LPDGADVSLS FSGDDPRLVI QAGRSRFNLP VLPAGDFPVM
SSDGLSSRIA VDTNELIRLI DKTRFAISTE ETRYYLNGLY VHTVNEGGET KLRAVATDGH
RLALAEMPAP EGAVGIPGVI VPRKTIAEAR RLMESAGETV DLQVSPQKVR FEFGAAALTS
KVIDGAFPDY MRVIPRDNAK ILTLDNDLFA KAVDRVATIS AEKSRSVKLA VEPGRITLTV
RNMEAGQAVE EVEVDYDGEP FEIGFNARYL LDVCGQIAGP QAEFRFADPA SPTLVVDPVD
PGVKYVLMPL RV
