ID   GRIR_STRM4              Reviewed;         373 AA.
AC   A0A0E3URH8;
DT   30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT   24-JUN-2015, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=Beta sliding clamp homolog GriR {ECO:0000303|PubMed:26045430};
DE            Short=Beta clamp GriR;
DE            Short=Sliding clamp GriR;
GN   Name=griR {ECO:0000303|PubMed:26045430};
GN   Synonyms=dnaN2 {ECO:0000305|PubMed:26045430};
OS   Streptomyces muensis.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1077944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND ANTIBIOTIC-BINDING.
RC   STRAIN=DSM 40835 / JCM 4881 / NRRL 2957 / CGMCC 4.1390 / DS 9461;
RX   PubMed=26045430; DOI=10.1126/science.aaa4690;
RA   Kling A., Lukat P., Almeida D.V., Bauer A., Fontaine E., Sordello S.,
RA   Zaburannyi N., Herrmann J., Wenzel S.C., Konig C., Ammerman N.C.,
RA   Barrio M.B., Borchers K., Bordon-Pallier F., Bronstrup M., Courtemanche G.,
RA   Gerlitz M., Geslin M., Hammann P., Heinz D.W., Hoffmann H., Klieber S.,
RA   Kohlmann M., Kurz M., Lair C., Matter H., Nuermberger E., Tyagi S.,
RA   Fraisse L., Grosset J.H., Lagrange S., Muller R.;
RT   "Targeting DnaN for tuberculosis therapy using novel griselimycins.";
RL   Science 348:1106-1112(2015).
CC   -!- FUNCTION: A homolog of the beta sliding clamp protein encoded within
CC       the biosynthetic cluster for griselimycin synthesis (PubMed:26045430).
CC       Upon expression in S.coelicolor A3(2), which is susceptible to this
CC       antibiotic, confers resistance to griselimycin (PubMed:26045430). The
CC       beta sliding clamp confers DNA tethering and processivity to DNA
CC       polymerases and other proteins (By similarity). Acts as a clamp,
CC       forming a ring around DNA (a reaction catalyzed by the clamp-loading
CC       complex) which diffuses in an ATP-independent manner freely and
CC       bidirectionally along dsDNA (By similarity). Initially characterized
CC       for its ability to contact the catalytic subunit of DNA polymerase III
CC       (Pol III), a complex, multichain enzyme responsible for most of the
CC       replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease
CC       proofreading activity (By similarity). The beta chain is required for
CC       initiation of replication as well as for processivity of DNA
CC       replication (By similarity). {ECO:0000250|UniProtKB:P0A988,
CC       ECO:0000269|PubMed:26045430}.
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; KP211414; AKC91855.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0E3URH8; -.
DR   SMR; A0A0E3URH8; -.
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   GO; GO:0046677; P:response to antibiotic; 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   Antibiotic resistance; Cytoplasm; DNA replication; DNA-binding;
KW   DNA-directed DNA polymerase; Nucleotidyltransferase; Transferase.
FT   CHAIN           1..373
FT                   /note="Beta sliding clamp homolog GriR"
FT                   /id="PRO_0000441111"
SQ   SEQUENCE   373 AA;  40334 MW;  46A42DBFD8661779 CRC64;
     MRFQVEREVL AEGIGWVARG LAVRPSVPIL SGVVVNAEGD TLTLSGFDYE VSTRVELKAN
     VEESGTVLIP GRRLADIAKV LPDVPIEFNV DQTKVYVQCD SNSFVLNALP LDEYPTLPKL
     PTVCGSVEGD QFARAVSQVA VVASRDDALP VLTGIGVNFD GEIMKLNATD RYRFAIRELA
     WKPEGTPSSS SVLVPARTLL DFAKSLNKGD LVKIALSDEG NLLGLHAGTR QMTCRLLEGT
     LPDYEKLFPK EFTSFGAVEV SRLVEALKRV SLVLERNSSV ALDFTDGELV LQAGGADDDR
     ATSRMAASLE GESIDIAFNP SFLLDGLTNL DASWAQFSFT SSNGKAVIMG KSSVDAEADT
     SARYLVMPVR FHR