ID Q73M89_TREDE Unreviewed; 667 AA.
AC Q73M89;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=UvrD-like helicase ATP-binding domain-containing protein {ECO:0000259|PROSITE:PS51198};
GN OrderedLocusNames=TDE_1620 {ECO:0000313|EMBL:AAS12137.1};
OS Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS / KCTC 15104).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=243275 {ECO:0000313|EMBL:AAS12137.1, ECO:0000313|Proteomes:UP000008212};
RN [1] {ECO:0000313|EMBL:AAS12137.1, ECO:0000313|Proteomes:UP000008212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104
RC {ECO:0000313|Proteomes:UP000008212};
RX PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA Seshadri R., Myers G.S., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA Ren Q., Brinkac L.M., Madupu R., Kolonay J., Durkin S.A., Daugherty S.C.,
RA Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G., Malek J.,
RA Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K., Pal S.,
RA Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E., Baca E.,
RA Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT "Comparison of the genome of the oral pathogen Treponema denticola with
RT other spirochete genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
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DR EMBL; AE017226; AAS12137.1; -; Genomic_DNA.
DR RefSeq; NP_972226.1; NC_002967.9.
DR RefSeq; WP_002679307.1; NC_002967.9.
DR AlphaFoldDB; Q73M89; -.
DR STRING; 243275.TDE_1620; -.
DR PaxDb; 243275-TDE_1620; -.
DR GeneID; 2740861; -.
DR KEGG; tde:TDE_1620; -.
DR PATRIC; fig|243275.7.peg.1548; -.
DR eggNOG; COG0210; Bacteria.
DR HOGENOM; CLU_004585_8_1_12; -.
DR OrthoDB; 1100019at2; -.
DR Proteomes; UP000008212; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000008212}.
FT DOMAIN 21..319
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT REGION 281..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 42..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 667 AA; 76499 MW; 8E85A61319D8CD64 CRC64;
MQITITNEDI EYAEKILLPA NKHFDEERRN FITNLDTIDL QAVPGSGKTT ALLAKLIILE
KKMPFPDGSG VLILSHTNTA VEEIQSKLQT IAPKLFNFPN FVGTIQSFTD TFLALPYYAH
VHKTHPYRID DDIYFRRCEL ALKYKYSSLT WFSYRPHKVQ MTTLLTAKID QNGCAKCING
LKNLKCSTAI KIAQFKYDNV KKGFLTYNDA FEFANFYIND NPRIVSIFQK RFKYVFVDEM
QDMHSHQIKL LDALFYTSGH TDEQQTITVF QRIGDVNQSI FGENDSDNSD GSTEKADNSG
KADWKPREHL TLLGSHRLSP CTAAIVSSFA VEPNAIQGLR KNADGTAIDI KPYLFVYKKE
NIKTVIKKFA HLIYKLQNEG KLPMTGSYAA VGWRKSILDD AADNKLGISD YYDSLCAAAA
STKINYSSLT DHLLAVDPHK KHLETMRKSI LNALLHILYM QKIQDKHGRY YTIRTLFKYL
KEETDIYELF KRNLFRWCKQ RINSEPVEQT IHNIQAFLPD FLQAVSLDNN LININNDTYL
FITNPTTIIQ NNKPTGQEQI NTYSISGIDI SIKTVHAIKG QTVTGLLYME TYNSSMHESN
RLVDCFIHKK FRKTAKTKKS GMMYKAAKTV YVGFSRPTHL LCFAVQKERF DKYLSNIDRA
VWDIIDI
//