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DPO3B_RICBR
ID   DPO3B_RICBR             Reviewed;         379 AA.
AC   Q1RIS7;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=RBE_0656;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A988}.
CC   -!- SIMILARITY: Belongs to the beta sliding clamp family. {ECO:0000305}.
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DR   EMBL; CP000087; ABE04737.1; -; Genomic_DNA.
DR   RefSeq; WP_011477325.1; NC_007940.1.
DR   PDB; 6MAN; X-ray; 2.35 A; A/B=1-379.
DR   PDBsum; 6MAN; -.
DR   AlphaFoldDB; Q1RIS7; -.
DR   SMR; Q1RIS7; -.
DR   STRING; 336407.RBE_0656; -.
DR   EnsemblBacteria; ABE04737; ABE04737; RBE_0656.
DR   KEGG; rbe:RBE_0656; -.
DR   eggNOG; COG0592; Bacteria.
DR   HOGENOM; CLU_038149_4_2_5; -.
DR   OMA; YLIMPVR; -.
DR   OrthoDB; 1040142at2; -.
DR   Proteomes; UP000001951; 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   3D-structure; Cytoplasm; DNA replication; DNA-binding;
KW   DNA-directed DNA polymerase; Nucleotidyltransferase; Transferase.
FT   CHAIN           1..379
FT                   /note="Beta sliding clamp"
FT                   /id="PRO_0000280790"
FT   STRAND          3..7
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   HELIX           8..21
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   HELIX           29..32
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   STRAND          33..39
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   STRAND          42..48
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   STRAND          50..59
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   STRAND          61..64
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   STRAND          66..71
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   HELIX           72..79
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   STRAND          85..91
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   HELIX           93..95
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   STRAND          97..101
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   STRAND          104..108
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   STRAND          125..131
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   HELIX           132..140
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   HELIX           143..145
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   HELIX           153..155
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   STRAND          156..163
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   STRAND          166..172
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   STRAND          174..183
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   STRAND          191..196
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   HELIX           197..208
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   TURN            210..214
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   STRAND          215..221
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   STRAND          223..230
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   TURN            231..233
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   STRAND          234..239
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   HELIX           248..251
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   STRAND          258..263
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   HELIX           264..275
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   STRAND          285..289
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   STRAND          291..300
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   TURN            301..303
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   STRAND          304..311
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   HELIX           316..318
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   STRAND          320..323
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   STRAND          328..332
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   HELIX           334..341
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   STRAND          347..353
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   STRAND          360..364
FT                   /evidence="ECO:0007829|PDB:6MAN"
FT   STRAND          367..374
FT                   /evidence="ECO:0007829|PDB:6MAN"
SQ   SEQUENCE   379 AA;  41849 MW;  1E25C4D4B9551B77 CRC64;
     MLKVIVETKT LVQALGFASS VVEKRNIISE LANIKLLAKD GLLELSSTNM DLYLSQKIGV
     QVVSEGELTV STKTLNDIVK KLPDSELTLT DLGTTGLEIT GKNCRFNLFT LPVESFPVMD
     NINPEASFKI SCAEFAKIIE STKFSVSLDE TRYNLNGIYL HVKDSEFYAA STDGHRLSVS
     SVVLAEKIED FGVILPQKSA EEILKIVKDS KNANADIEIL LSSNKIKFIC NENVIMLSKL
     IDGTFPDYSS FIPENSSSKL VINRKIFADT IERIAIITVE KFRAVKLSLS GEALEISAIG
     EARGNAKEVI NSSKETENFY EYSGETNLDI GFNPQYLEDV LKAIKSDLVE LYFSSVSAPV
     LIKFPESPKD IFVVMPVKV
 
 
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