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   27-MAR-2024, entry version 134.
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; Campylobacterota; 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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.HP_0500; -.
DR   PaxDb; 85962-C694_02570; -.
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   InParanoid; O25242; -.
DR   OrthoDB; 8421503at2; -.
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   Gene3D; 3.10.150.10; DNA Polymerase III, subunit A, domain 2; 3.
DR   InterPro; IPR046938; DNA_clamp_sf.
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   NCBIfam; TIGR00663; dnan; 1.
DR   PANTHER; PTHR30478:SF0; BETA SLIDING CLAMP; 1.
DR   PANTHER; PTHR30478; DNA POLYMERASE III SUBUNIT BETA; 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   SUPFAM; SSF55979; DNA clamp; 3.
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
//