ID G7CIP4_MYCT3 Unreviewed; 397 AA.
AC G7CIP4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Beta sliding clamp {ECO:0000256|PIRNR:PIRNR000804};
GN ORFNames=KEK_10778 {ECO:0000313|EMBL:EHI11373.1};
OS Mycolicibacterium thermoresistibile (strain ATCC 19527 / DSM 44167 / CIP
OS 105390 / JCM 6362 / NCTC 10409 / 316) (Mycobacterium thermoresistibile).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1078020 {ECO:0000313|EMBL:EHI11373.1, ECO:0000313|Proteomes:UP000004915};
RN [1] {ECO:0000313|EMBL:EHI11373.1, ECO:0000313|Proteomes:UP000004915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19527 / DSM 44167 / CIP 105390 / JCM 6362 / NCTC 10409 /
RC 316 {ECO:0000313|Proteomes:UP000004915};
RG Tuberculosis Structural Genomics Consortium;
RA Ioerger T.R.;
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007829|PDB:8DJ6, ECO:0007829|PDB:8DK9}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS).
RA Kapur M.K., Gray O.J., Honzatko R.H., Nelson S.N.;
RT "Interaction of sliding clamp with mycobacterial polymerases.";
RL Submitted (JUL-2022) to the PDB data bank.
RN [3] {ECO:0007829|PDB:8DJQ}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS).
RA Kapur M.K., Gray O.J., Honzatko R.H., Nelson S.N.;
RT "Interaction of the sliding clamp with mycobacterial polymerases.";
RL Submitted (JUL-2022) to the PDB data bank.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHI11373.1}.
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DR EMBL; AGVE01000046; EHI11373.1; -; Genomic_DNA.
DR RefSeq; WP_003925639.1; NZ_AGVE01000046.1.
DR PDB; 8DJ6; X-ray; 2.50 A; A/B/C/D=1-397.
DR PDB; 8DJQ; X-ray; 2.80 A; A/B/C/D=1-397.
DR PDB; 8DK9; X-ray; 2.50 A; A/B/C/D=1-397.
DR PDB; 8DKD; X-ray; 3.20 A; A=1-397.
DR AlphaFoldDB; G7CIP4; -.
DR SMR; G7CIP4; -.
DR PATRIC; fig|1078020.3.peg.2112; -.
DR eggNOG; COG0592; Bacteria.
DR Proteomes; UP000004915; Unassembled WGS sequence.
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; 3.10.150.10; DNA Polymerase III, subunit A, domain 2; 3.
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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:8DJ6, ECO:0007829|PDB:8DJQ};
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:UP000004915};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000804}.
FT DOMAIN 12..128
FT /note="DNA polymerase III beta sliding clamp N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00712"
FT DOMAIN 137..258
FT /note="DNA polymerase III beta sliding clamp central"
FT /evidence="ECO:0000259|Pfam:PF02767"
FT DOMAIN 260..371
FT /note="DNA polymerase III beta sliding clamp C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02768"
SQ SEQUENCE 397 AA; 41640 MW; DA1E016AFD1F2A20 CRC64;
MATTTVGLTD LKVRLVRDDF ADAVAWVARS LPSRPTVPVL AGVLLTGSDD GLTISSFDYE
VSAEVQIPAE IAAPGTVLVS GRLLSEITRA LPNKPVDLSV EGTRVSLTCG SARFSLPTMA
VEDYPALPEL PAETGSVPAD LFAEAIGQVA VAAGRDDTLP MLTGIRVEIS GDRMVLAATD
RFRLAVRELT WTTKTPDVEA AVLVPAKTLA EAAKTGLDGS EVQLALGAGP SVGQDGLLGI
RSEGKRSTTR LLDAEFPKFR QLLPTEHTAM ATIGVGELTE AIKRVALVAD RGAQVRMEFA
DDVLHLSAGA DDVGRAEEDL PVSFSGEPLT IAFNPGYLTD GLGALHSERV TFGFTTPSKP
AVLRPATEAD AALNGNGPFP AAETDYVYLL MPVRLPG
//
