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Database: UniProt
Entry: A0A449B4T7_9MOLU
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ID   A0A449B4T7_9MOLU        Unreviewed;       370 AA.
AC   A0A449B4T7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=DNA polymerase III, beta subunit {ECO:0000313|EMBL:VEU75621.1};
DE            EC=2.7.7.7 {ECO:0000313|EMBL:VEU75621.1};
GN   Name=dnaN {ECO:0000313|EMBL:VEU75621.1};
GN   ORFNames=NCTC10168_00548 {ECO:0000313|EMBL:VEU75621.1};
OS   Mycoplasmopsis maculosa.
OC   Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=114885 {ECO:0000313|EMBL:VEU75621.1, ECO:0000313|Proteomes:UP000290243};
RN   [1] {ECO:0000313|EMBL:VEU75621.1, ECO:0000313|Proteomes:UP000290243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC10168 {ECO:0000313|EMBL:VEU75621.1,
RC   ECO:0000313|Proteomes:UP000290243};
RG   Pathogen Informatics;
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00011400}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the beta sliding clamp family.
CC       {ECO:0000256|ARBA:ARBA00010752}.
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DR   EMBL; LR215037; VEU75621.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A449B4T7; -.
DR   KEGG; mmau:NCTC10168_00548; -.
DR   OrthoDB; 397417at2; -.
DR   Proteomes; UP000290243; Chromosome 1.
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-EC.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd00140; beta_clamp; 1.
DR   Gene3D; 3.70.10.10; -; 1.
DR   Gene3D; 3.10.150.10; DNA Polymerase III, subunit A, domain 2; 1.
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   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:VEU75621.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000290243};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:VEU75621.1}.
FT   DOMAIN          1..124
FT                   /note="DNA polymerase III beta sliding clamp N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00712"
FT   DOMAIN          133..240
FT                   /note="DNA polymerase III beta sliding clamp central"
FT                   /evidence="ECO:0000259|Pfam:PF02767"
FT   DOMAIN          255..369
FT                   /note="DNA polymerase III beta sliding clamp C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02768"
SQ   SEQUENCE   370 AA;  42580 MW;  9FB6DD4069A205F5 CRC64;
     MHIIIKKNII DEIIEIVSKF TDPISSFYGM RCILINTDDN KITFKATNEI TNIIKSIDVD
     NTDVIVKKPG EILIQANIFK NIIKKLNGFI EIEKISNSNL IEIKQDSSRY TLNTSDVKTF
     PKIDESTNTK EIEINTDNFK KAVKNVAFAA SNENNLIYKC INFRSNGNKL NLTATDSYRL
     AFYTINTNYV LDDFEFSVNA KDVKDLIPSD APKVVKLFYN SIKVGIKYDN TVITSRITDL
     PYHDIESLFT KVMSETKYKV TINKNELNNL LNKIWIGTND KQNRIEIKIK KNELSIFTKL
     DEIGDSFVKT ENLELEGSNL EFDINYNYLK EALSVFDDEL YILVDEKIQK ILIISKSNPN
     TKQLISPMRR
//
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