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Database: UniProt
Entry: G4STN4_META2
LinkDB: G4STN4_META2
Original site: G4STN4_META2 
ID   G4STN4_META2            Unreviewed;       366 AA.
AC   G4STN4;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Beta sliding clamp {ECO:0000256|ARBA:ARBA00021035, ECO:0000256|PIRNR:PIRNR000804};
GN   Name=dnaN {ECO:0000313|EMBL:CCE21706.1};
GN   OrderedLocusNames=MEALZ_0002 {ECO:0000313|EMBL:CCE21706.1};
OS   Methylotuvimicrobium alcaliphilum (strain DSM 19304 / NCIMB 14124 / VKM
OS   B-2133 / 20Z) (Methylomicrobium alcaliphilum).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylotuvimicrobium.
OX   NCBI_TaxID=1091494 {ECO:0000313|EMBL:CCE21706.1, ECO:0000313|Proteomes:UP000008315};
RN   [1] {ECO:0000313|EMBL:CCE21706.1, ECO:0000313|Proteomes:UP000008315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z
RC   {ECO:0000313|Proteomes:UP000008315};
RX   PubMed=22207753; DOI=10.1128/JB.06392-11;
RA   Vuilleumier S., Khmelenina V.N., Bringel F., Reshetnikov A.S., Lajus A.,
RA   Mangenot S., Rouy Z., Op den Camp H.J., Jetten M.S., Dispirito A.A.,
RA   Dunfield P., Klotz M.G., Semrau J.D., Stein L.Y., Barbe V., Medigue C.,
RA   Trotsenko Y.A., Kalyuzhnaya M.G.;
RT   "Genome sequence of the haloalkaliphilic methanotrophic bacterium
RT   Methylomicrobium alcaliphilum 20Z.";
RL   J. Bacteriol. 194:551-552(2012).
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: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|ARBA:ARBA00004496,
CC       ECO:0000256|PIRNR:PIRNR000804}.
CC   -!- SIMILARITY: Belongs to the beta sliding clamp family.
CC       {ECO:0000256|ARBA:ARBA00010752, ECO:0000256|PIRNR:PIRNR000804}.
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DR   EMBL; FO082060; CCE21706.1; -; Genomic_DNA.
DR   RefSeq; WP_014146524.1; NC_016112.1.
DR   AlphaFoldDB; G4STN4; -.
DR   STRING; 1091494.MEALZ_0002; -.
DR   KEGG; mah:MEALZ_0002; -.
DR   PATRIC; fig|271065.3.peg.2; -.
DR   HOGENOM; CLU_038149_4_2_6; -.
DR   Proteomes; UP000008315; 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   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   PIRSF; PIRSF000804; DNA_pol_III_b; 1.
DR   SMART; SM00480; POL3Bc; 1.
DR   SUPFAM; SSF55979; DNA clamp; 3.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR000804};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|PIRNR:PIRNR000804};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|PIRNR:PIRNR000804};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|PIRNR:PIRNR000804};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008315};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000804}.
FT   DOMAIN          1..117
FT                   /note="DNA polymerase III beta sliding clamp N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00712"
FT   DOMAIN          129..243
FT                   /note="DNA polymerase III beta sliding clamp central"
FT                   /evidence="ECO:0000259|Pfam:PF02767"
FT   DOMAIN          246..365
FT                   /note="DNA polymerase III beta sliding clamp C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02768"
SQ   SEQUENCE   366 AA;  41562 MW;  7B5192EDCF14918A CRC64;
     MKYIINREQL LVPLQQIVSV IEKRQTMPIL SNVLMVFRQN SLLMTGTDLE VQIVTEIAIE
     NTTFAEITLP ARKFLDICRL LPTGADIKLE VADDKVKVLS GRSRFILSTL PAENYPEFSE
     TELDHRFTIN AGLFKKALEK TVFCMASQDV RYYLNGLLLN ISNSRIKLVA SDGHRLSVFE
     DNLENPAGYE ARIILPRKGV MELVRLLDDP EIELAVEFSS NNIRVTINNT IFSAKLVDAK
     YPDFNRVFHQ DFLTPIHIQR QLLKDALTRV AILSNEKYKG VTFDLSSDSL KISAHNPEHE
     EAEEEIVTDY VGEPLSIAFN VQYVLDAISN IDSEISELTI ASNSSCCIID EPETRSYRFI
     VMPMRL
//
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