DPO3B_MYCS2
ID DPO3B_MYCS2 Reviewed; 397 AA.
AC A0QND6; I7FC80;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 117.
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=MSMEG_0001, MSMEI_0003;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4] {ECO:0007744|PDB:5AH2, ECO:0007744|PDB:5AH4}
RP X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS) IN COMPLEX WITH ANTIBIOTICS,
RP SUBUNIT, AND ANTIBIOTIC-BINDING.
RC STRAIN=ATCC 700084 / mc(2)155;
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: 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 (PubMed:26045430)
CC around DNA which binds and tethers DNA polymerases and other proteins
CC to the DNA (By similarity). The DNA replisome complex has a single
CC clamp-loading complex (3 tau and 1 each of delta, delta', psi and chi
CC subunits) which binds 3 Pol III cores (1 core on the leading strand and
CC 2 on the lagging strand) each with a beta sliding clamp dimer (By
CC similarity). Additional proteins in the replisome are other copies of
CC gamma, psi and chi, Ssb, DNA helicase and RNA primase (By similarity).
CC {ECO:0000250|UniProtKB:P0A988, ECO:0000269|PubMed:26045430}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A988}.
CC -!- MISCELLANEOUS: Strains that are resistant to griselimycin occur at a
CC very low frequency (5 x 10(-10)) and are associated with amplification
CC of a chromosomal segment containing this gene as well as the ori site
CC (with a single point mutation in the promoter region), suggesting
CC antibiotic resistance may be due to overexpression of the protein
CC (PubMed:26045430). {ECO:0000269|PubMed:26045430}.
CC -!- SIMILARITY: Belongs to the beta sliding clamp family. {ECO:0000305}.
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DR EMBL; CP000480; ABK70300.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP36488.1; -; Genomic_DNA.
DR RefSeq; WP_011726602.1; NZ_SIJM01000001.1.
DR RefSeq; YP_884424.1; NC_008596.1.
DR PDB; 5AH2; X-ray; 2.13 A; A/B/C/D=1-397.
DR PDB; 5AH4; X-ray; 2.31 A; A/B=1-397.
DR PDBsum; 5AH2; -.
DR PDBsum; 5AH4; -.
DR AlphaFoldDB; A0QND6; -.
DR SMR; A0QND6; -.
DR DIP; DIP-61661N; -.
DR IntAct; A0QND6; 1.
DR STRING; 246196.MSMEI_0003; -.
DR PRIDE; A0QND6; -.
DR EnsemblBacteria; ABK70300; ABK70300; MSMEG_0001.
DR EnsemblBacteria; AFP36488; AFP36488; MSMEI_0003.
DR GeneID; 66738193; -.
DR KEGG; msg:MSMEI_0003; -.
DR KEGG; msm:MSMEG_0001; -.
DR PATRIC; fig|246196.19.peg.1; -.
DR eggNOG; COG0592; Bacteria.
DR OMA; YLIMPVR; -.
DR OrthoDB; 1040142at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 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 3D-structure; Antibiotic resistance; Cytoplasm; DNA replication;
KW DNA-binding; DNA-directed DNA polymerase; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..397
FT /note="Beta sliding clamp"
FT /id="PRO_0000441110"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:5AH2"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:5AH2"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:5AH2"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:5AH2"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:5AH2"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:5AH2"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:5AH2"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:5AH2"
FT HELIX 81..90
FT /evidence="ECO:0007829|PDB:5AH2"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:5AH2"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:5AH2"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:5AH2"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:5AH4"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:5AH2"
FT HELIX 139..150
FT /evidence="ECO:0007829|PDB:5AH2"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:5AH2"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:5AH2"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:5AH2"
FT STRAND 181..190
FT /evidence="ECO:0007829|PDB:5AH2"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:5AH2"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:5AH2"
FT HELIX 206..215
FT /evidence="ECO:0007829|PDB:5AH2"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:5AH2"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:5AH2"
FT TURN 232..235
FT /evidence="ECO:0007829|PDB:5AH2"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:5AH2"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:5AH2"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:5AH2"
FT STRAND 265..274
FT /evidence="ECO:0007829|PDB:5AH2"
FT HELIX 275..285
FT /evidence="ECO:0007829|PDB:5AH2"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:5AH2"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:5AH2"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:5AH2"
FT STRAND 303..310
FT /evidence="ECO:0007829|PDB:5AH2"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:5AH2"
FT STRAND 314..321
FT /evidence="ECO:0007829|PDB:5AH2"
FT STRAND 323..327
FT /evidence="ECO:0007829|PDB:5AH2"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:5AH2"
FT HELIX 335..345
FT /evidence="ECO:0007829|PDB:5AH2"
FT STRAND 347..356
FT /evidence="ECO:0007829|PDB:5AH2"
FT STRAND 361..365
FT /evidence="ECO:0007829|PDB:5AH2"
FT STRAND 385..390
FT /evidence="ECO:0007829|PDB:5AH2"
SQ SEQUENCE 397 AA; 41325 MW; 1D183DE63956CFED CRC64;
MATTTAGLTD LKFRVVREDF ADAVAWVARS LPTRPTIPVL AGVLLTGTDE GLTISGFDYE
VSAEVKVSAE IASAGSVLVS GRLLSDITKA LPAKPVEVSV EGTRVSLTCG SARFSLPTLA
VEDYPALPAL PEETGVIASD LFAEAIGQVA VAAGRDDTLP MLTGIRVEIS GESVVLAATD
RFRLAVRELT WVTTAGDVEA AVLVPAKTLA EAAKAGTDGN QVHLALGSGA SVGKDGLLGI
RSEGKRSTTR LLDAEFPKFR QLLPAEHTAV ATIGVAELTE AIKRVALVAD RGAQIRMEFS
DDTLKLSAGA DDVGRAEEDL PVDFAGEPLT IAFNPTYLTD GLGSLHSERV TFGFTTPSRP
AVLRPAGEDD GANGGSGPFP AAKTDYVYLL MPVRLPG
