DPO3B_PSEAE
ID DPO3B_PSEAE Reviewed; 367 AA.
AC Q9I7C4;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=PA0002;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2] {ECO:0007744|PDB:4TR8, ECO:0007744|PDB:4TSZ}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) ALONE AND IN COMPLEX WITH PEPTIDE,
RP 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 around DNA which
CC binds and tethers DNA polymerases and other proteins to the DNA
CC (PubMed:25170813). 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 (By similarity).
CC {ECO:0000250|UniProtKB:P0A988, ECO:0000269|PubMed:25170813}.
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; AE004091; AAG03392.1; -; Genomic_DNA.
DR PIR; F83644; F83644.
DR RefSeq; NP_064722.1; NC_002516.2.
DR RefSeq; WP_003097262.1; NZ_QZGE01000012.1.
DR PDB; 4TR8; X-ray; 1.80 A; A/B=1-367.
DR PDB; 4TSZ; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-367.
DR PDB; 6AMS; X-ray; 2.39 A; A/B/C/D=1-367.
DR PDB; 6PTH; X-ray; 3.05 A; A=1-367.
DR PDBsum; 4TR8; -.
DR PDBsum; 4TSZ; -.
DR PDBsum; 6AMS; -.
DR PDBsum; 6PTH; -.
DR AlphaFoldDB; Q9I7C4; -.
DR SMR; Q9I7C4; -.
DR STRING; 287.DR97_2951; -.
DR PaxDb; Q9I7C4; -.
DR PRIDE; Q9I7C4; -.
DR DNASU; 879244; -.
DR EnsemblBacteria; AAG03392; AAG03392; PA0002.
DR GeneID; 879244; -.
DR KEGG; pae:PA0002; -.
DR PATRIC; fig|208964.12.peg.2; -.
DR PseudoCAP; PA0002; -.
DR HOGENOM; CLU_038149_4_2_6; -.
DR InParanoid; Q9I7C4; -.
DR OMA; YLIMPVR; -.
DR PhylomeDB; Q9I7C4; -.
DR BioCyc; PAER208964:G1FZ6-2-MON; -.
DR Proteomes; UP000002438; 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; ISS:PseudoCAP.
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..367
FT /note="Beta sliding clamp"
FT /id="PRO_0000105453"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:4TR8"
FT HELIX 7..19
FT /evidence="ECO:0007829|PDB:4TR8"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:4TR8"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:4TR8"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:4TR8"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:4TR8"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:4TR8"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:4TR8"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:4TR8"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:4TR8"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:4TR8"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:4TR8"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:4TR8"
FT HELIX 132..140
FT /evidence="ECO:0007829|PDB:4TR8"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:4TR8"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:4TR8"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:4TR8"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:4TR8"
FT STRAND 174..183
FT /evidence="ECO:0007829|PDB:4TR8"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:4TR8"
FT HELIX 198..207
FT /evidence="ECO:0007829|PDB:4TR8"
FT STRAND 214..227
FT /evidence="ECO:0007829|PDB:4TR8"
FT STRAND 229..236
FT /evidence="ECO:0007829|PDB:4TR8"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:4TR8"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:4TR8"
FT HELIX 261..272
FT /evidence="ECO:0007829|PDB:4TR8"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:4TR8"
FT STRAND 281..287
FT /evidence="ECO:0007829|PDB:4TR8"
FT STRAND 290..296
FT /evidence="ECO:0007829|PDB:4TR8"
FT STRAND 302..308
FT /evidence="ECO:0007829|PDB:4TR8"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:4TR8"
FT HELIX 322..331
FT /evidence="ECO:0007829|PDB:4TR8"
FT STRAND 334..341
FT /evidence="ECO:0007829|PDB:4TR8"
FT STRAND 348..354
FT /evidence="ECO:0007829|PDB:4TR8"
FT STRAND 356..362
FT /evidence="ECO:0007829|PDB:4TR8"
SQ SEQUENCE 367 AA; 40694 MW; 7E94B6593020CBA2 CRC64;
MHFTIQREAL LKPLQLVAGV VERRQTLPVL SNVLLVVEGQ QLSLTGTDLE VELVGRVVLE
DAAEPGEITV PARKLMDICK SLPNDVLIDI RVEEQKLLVK AGRSRFTLST LPANDFPTVE
EGPGSLNFSI AQSKLRRLID RTSFAMAQQD VRYYLNGMLL EVNGGTLRSV ATDGHRLAMC
SLDAQIPSQD RHQVIVPRKG ILELARLLTE QDGEVGIVLG QHHIRATTGE FTFTSKLVDG
KFPDYERVLP RGGDKLVVGD RQQLREAFSR TAILSNEKYR GIRLQLSNGL LKIQANNPEQ
EEAEEEVQVE YNGGNLEIGF NVSYLLDVLG VIGTEQVRFI LSDSNSSALV HEADNDDSAY
VVMPMRL
