(data stored in SCRATCH zone)

SWISSPROT: B4SU12_STRM5

ID   B4SU12_STRM5            Unreviewed;       366 AA.
AC   B4SU12;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 67.
DE   RecName: Full=Beta sliding clamp {ECO:0000256|PIRNR:PIRNR000804};
GN   OrderedLocusNames=Smal_0002 {ECO:0000313|EMBL:ACF49707.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF49707.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF49707.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF49707.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Confers DNA tethering and processivity to DNA
CC       polymerases and other proteins. Acts as a clamp, forming a ring
CC       around DNA (a reaction catalyzed by the clamp-loading complex)
CC       which diffuses in an ATP-independent manner freely and
CC       bidirectionally along dsDNA. Initially characterized for its
CC       ability to contact the catalytic subunit of DNA polymerase III
CC       (Pol III), a complex, multichain enzyme responsible for most of
CC       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:0000256|PIRNR:PIRNR000804}.
CC   -!- SUBUNIT: Forms a ring-shaped head-to-tail homodimer around DNA.
CC       {ECO:0000256|PIRNR:PIRNR000804}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR000804,
CC       ECO:0000256|SAAS:SAAS00729396}.
CC   -!- SIMILARITY: Belongs to the beta sliding clamp family.
CC       {ECO:0000256|PIRNR:PIRNR000804, ECO:0000256|SAAS:SAAS00859809}.
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DR   EMBL; CP001111; ACF49707.1; -; Genomic_DNA.
DR   RefSeq; WP_006404569.1; NC_011071.1.
DR   STRING; 391008.Smal_0002; -.
DR   EnsemblBacteria; ACF49707; ACF49707; Smal_0002.
DR   KEGG; smt:Smal_0002; -.
DR   eggNOG; ENOG4105CZ8; Bacteria.
DR   eggNOG; COG0592; LUCA.
DR   HOGENOM; HOG000071791; -.
DR   KO; K02338; -.
DR   OMA; NYEAVIP; -.
DR   OrthoDB; 1040142at2; -.
DR   BioCyc; SMAL391008:SMAL_RS00010-MONOMER; -.
DR   Proteomes; UP000001867; 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-UniRule.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
DR   PRODOM; B4SU12.
DR   SWISS-2DPAGE; B4SU12.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR000804,
KW   ECO:0000256|SAAS:SAAS00729481};
KW   DNA replication {ECO:0000256|PIRNR:PIRNR000804,
KW   ECO:0000256|SAAS:SAAS00729460};
KW   DNA-binding {ECO:0000256|SAAS:SAAS00859811};
KW   DNA-directed DNA polymerase {ECO:0000256|PIRNR:PIRNR000804,
KW   ECO:0000256|SAAS:SAAS00729479};
KW   Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR000804,
KW   ECO:0000256|SAAS:SAAS00729386, ECO:0000313|EMBL:ACF49707.1};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000804,
KW   ECO:0000256|SAAS:SAAS00729371, ECO:0000313|EMBL:ACF49707.1}.
FT   DOMAIN        1    118       DNA_pol3_beta. {ECO:0000259|Pfam:
FT                                PF00712}.
FT   DOMAIN      130    243       DNA_pol3_beta_2. {ECO:0000259|Pfam:
FT                                PF02767}.
FT   DOMAIN      247    365       DNA_pol3_beta_3. {ECO:0000259|Pfam:
FT                                PF02768}.
SQ   SEQUENCE   366 AA;  40771 MW;  1C24AD072989A2A8 CRC64;
     MRFTLQREAF LKPLAQVVNV VERRQTLPVL ANFLVQVQNG QLSLTGTDLE VEMVSRIAVE
     DAQDGETTIP ARKLFEIIRA LPDGSRITVS QTGDKITVQA GRSRFTLATL PSNDFPSVDE
     VEATERVAIG EATLKELIER TAFAMAQQDV RYYLNGLLFD LRGDALRTVA TDGHRLALCE
     TDLAKPSGSK RQIIVPRKGV TELQRLLESG DREIELEVGR SHVRVKRDDV TFTSKLIDGR
     FPDYEAVIPI GADREVKVNR ESLRASLQRA AILSNEKYRG IRVEVSPGNL KISAHNPEQE
     EAQEEIEADT TVSDLAIGFN VNYLLDALSA LRDEEVIIQL RDSNSSALVR ESSSEKSRHV
     VMPLRL
//

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