DPO3B_HELPY
ID DPO3B_HELPY Reviewed; 374 AA.
AC O25242;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 126.
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=HP_0500;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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 -!- INTERACTION:
CC O25242; O25172: HP_0418; NbExp=3; IntAct=EBI-7532786, EBI-9262675;
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; AE000511; AAD07565.1; -; Genomic_DNA.
DR PIR; D64582; D64582.
DR RefSeq; NP_207297.1; NC_000915.1.
DR RefSeq; WP_000704186.1; NC_018939.1.
DR PDB; 4RKI; X-ray; 2.05 A; A=1-374.
DR PDB; 4S3I; X-ray; 1.95 A; A/B=1-374.
DR PDB; 5FRQ; X-ray; 2.90 A; A/B/C/D=1-374.
DR PDB; 5FVE; X-ray; 2.07 A; A=1-374.
DR PDB; 5FXT; X-ray; 1.97 A; A=1-374.
DR PDB; 5G48; X-ray; 2.28 A; A/B=1-374.
DR PDB; 5G4Q; X-ray; 2.30 A; A/B=1-374.
DR PDBsum; 4RKI; -.
DR PDBsum; 4S3I; -.
DR PDBsum; 5FRQ; -.
DR PDBsum; 5FVE; -.
DR PDBsum; 5FXT; -.
DR PDBsum; 5G48; -.
DR PDBsum; 5G4Q; -.
DR AlphaFoldDB; O25242; -.
DR SMR; O25242; -.
DR DIP; DIP-3288N; -.
DR IntAct; O25242; 2.
DR MINT; O25242; -.
DR STRING; 85962.C694_02570; -.
DR PaxDb; O25242; -.
DR DNASU; 899259; -.
DR EnsemblBacteria; AAD07565; AAD07565; HP_0500.
DR KEGG; hpy:HP_0500; -.
DR PATRIC; fig|85962.47.peg.538; -.
DR eggNOG; COG0592; Bacteria.
DR OMA; YLIMPVR; -.
DR PhylomeDB; O25242; -.
DR Proteomes; UP000000429; 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 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..374
FT /note="Beta sliding clamp"
FT /id="PRO_0000105438"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:4S3I"
FT HELIX 7..17
FT /evidence="ECO:0007829|PDB:4S3I"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:4S3I"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:4S3I"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:4S3I"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:4S3I"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:4S3I"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:4S3I"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:4S3I"
FT HELIX 72..80
FT /evidence="ECO:0007829|PDB:4S3I"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:4S3I"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:4S3I"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:4S3I"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:4S3I"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:4S3I"
FT HELIX 133..141
FT /evidence="ECO:0007829|PDB:4S3I"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:4S3I"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:4S3I"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:4S3I"
FT TURN 163..166
FT /evidence="ECO:0007829|PDB:4S3I"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:4S3I"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:4S3I"
FT STRAND 188..200
FT /evidence="ECO:0007829|PDB:4S3I"
FT HELIX 201..210
FT /evidence="ECO:0007829|PDB:4S3I"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:4S3I"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:4S3I"
FT STRAND 229..236
FT /evidence="ECO:0007829|PDB:4S3I"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:4S3I"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:4S3I"
FT HELIX 261..271
FT /evidence="ECO:0007829|PDB:4S3I"
FT TURN 272..274
FT /evidence="ECO:0007829|PDB:4S3I"
FT STRAND 276..282
FT /evidence="ECO:0007829|PDB:4S3I"
FT STRAND 284..293
FT /evidence="ECO:0007829|PDB:4S3I"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:4S3I"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:4S3I"
FT HELIX 322..330
FT /evidence="ECO:0007829|PDB:4S3I"
FT STRAND 334..343
FT /evidence="ECO:0007829|PDB:4S3I"
FT STRAND 348..352
FT /evidence="ECO:0007829|PDB:4S3I"
FT TURN 353..356
FT /evidence="ECO:0007829|PDB:4S3I"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:5FXT"
FT STRAND 366..369
FT /evidence="ECO:0007829|PDB:4S3I"
SQ SEQUENCE 374 AA; 42185 MW; 5C1FE1C6290FDE6C CRC64;
MKISVSKNDL ENALRYLQAF LDKKDASSIA SHIHLEVIKE KLFLKASDSD IGLKSYIFTQ
SSDKEGVGTI NGKKFLDIIS CLKDSNIILE TKDDSLAIKQ NKSSFKLPMF DADEFPEFPV
IDPKVSIEVN APFLVDAFKK IAPVIEQTSH KRELAGILMQ FDQKHQTLSV VGTDTKRLSY
TQLEKISIHS TEEDISCILP KRALLEILKL FYENFSFKSD GMLAVIENEM HTFFTKLIDG
NYPDYQKILP KEYISSFTLG KEEFKESIKL CSSLSSTIKL TLEKNNALFE SLDSEHSETA
KTSVEIEKGL DIEKAFHLGV NAKFFLEALN ALGTTQFVLR CNEPSSPFLI QESLDEKQSH
LNAKISTLMM PITL
