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Database: UniProt
Entry: E0RN49_SPITD
LinkDB: E0RN49_SPITD
Original site: E0RN49_SPITD 
ID   E0RN49_SPITD            Unreviewed;       119 AA.
AC   E0RN49;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   SubName: Full=DNA polymerase, beta domain protein region {ECO:0000313|EMBL:ADN02518.1};
GN   OrderedLocusNames=STHERM_c15780 {ECO:0000313|EMBL:ADN02518.1};
OS   Spirochaeta thermophila (strain ATCC 49972 / DSM 6192 / RI 19.B1).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC   Spirochaeta.
OX   NCBI_TaxID=665571 {ECO:0000313|EMBL:ADN02518.1, ECO:0000313|Proteomes:UP000001296};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 6192;
RA   Angelov A., Mientus M., Wittenberg S., Lehmann R., Liesegang H., Daniel R.,
RA   Liebl W.;
RT   "The genome sequence of Spirochaeta thermophila DSM6192.";
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADN02518.1, ECO:0000313|Proteomes:UP000001296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49972 / DSM 6192 / RI 19.B1
RC   {ECO:0000313|Proteomes:UP000001296};
RX   PubMed=20935097; DOI=10.1128/JB.01023-10;
RA   Angelov A., Liebl S., Ballschmiter M., Bomeke M., Lehmann R., Liesegang H.,
RA   Daniel R., Liebl W.;
RT   "Genome sequence of the polysaccharide-degrading, thermophilic anaerobe
RT   Spirochaeta thermophila DSM 6192.";
RL   J. Bacteriol. 192:6492-6493(2010).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the MntA antitoxin family.
CC       {ECO:0000256|ARBA:ARBA00038276}.
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DR   EMBL; CP001698; ADN02518.1; -; Genomic_DNA.
DR   AlphaFoldDB; E0RN49; -.
DR   PaxDb; 665571-STHERM_c15780; -.
DR   KEGG; sta:STHERM_c15780; -.
DR   eggNOG; COG1669; Bacteria.
DR   HOGENOM; CLU_130257_10_0_12; -.
DR   OMA; YVRQEQT; -.
DR   Proteomes; UP000001296; Chromosome.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd05403; NT_KNTase_like; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR   PANTHER; PTHR33571:SF14; PROTEIN ADENYLYLTRANSFERASE MJ0128-RELATED; 1.
DR   PANTHER; PTHR33571; SSL8005 PROTEIN; 1.
DR   Pfam; PF01909; NTP_transf_2; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Toxin-antitoxin system {ECO:0000256|ARBA:ARBA00022649}.
FT   DOMAIN          33..113
FT                   /note="Polymerase nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01909"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   119 AA;  13826 MW;  08088F8565A02E12 CRC64;
     MLKEGSKKKQ HKGGELVPMK NEKMNRQELI SLLRTLKPVL EDRYRIRSIA LFGSFARDEQ
     SQSSDIDLLV EFEEEADLFD LVGASQYLER HLHRPVDLVS SRALRENLQE SVRKDVVFV
//
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