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Database: UniProt
Entry: Q8DTY6_STRMU
LinkDB: Q8DTY6_STRMU
Original site: Q8DTY6_STRMU 
ID   Q8DTY6_STRMU            Unreviewed;       733 AA.
AC   Q8DTY6;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 127.
DE   RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364053};
DE            EC=5.6.2.4 {ECO:0000256|RuleBase:RU364053};
GN   Name=pcrA {ECO:0000313|EMBL:AAN58865.1};
GN   OrderedLocusNames=SMU_1174 {ECO:0000313|EMBL:AAN58865.1};
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007 {ECO:0000313|EMBL:AAN58865.1, ECO:0000313|Proteomes:UP000002512};
RN   [1] {ECO:0000313|EMBL:AAN58865.1, ECO:0000313|Proteomes:UP000002512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159 {ECO:0000313|Proteomes:UP000002512};
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H., Lin S., Qian Y., Li S., Zhu H.,
RA   Najar F., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034618,
CC         ECO:0000256|RuleBase:RU364053};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC         translocating in the 3'-5' direction.; EC=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034617};
CC   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000256|ARBA:ARBA00009922, ECO:0000256|RuleBase:RU364053}.
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DR   EMBL; AE014133; AAN58865.1; -; Genomic_DNA.
DR   RefSeq; NP_721559.1; NC_004350.2.
DR   AlphaFoldDB; Q8DTY6; -.
DR   STRING; 210007.SMU_1174; -.
DR   KEGG; smu:SMU_1174; -.
DR   PATRIC; fig|210007.7.peg.1053; -.
DR   eggNOG; COG0210; Bacteria.
DR   HOGENOM; CLU_004585_5_2_9; -.
DR   OrthoDB; 9810135at2; -.
DR   PhylomeDB; Q8DTY6; -.
DR   Proteomes; UP000002512; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:InterPro.
DR   CDD; cd17932; DEXQc_UvrD; 1.
DR   CDD; cd18807; SF1_C_UvrD; 1.
DR   Gene3D; 1.10.10.160; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR005751; ATP-dep_DNA_helicase_PcrA.
DR   InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   NCBIfam; TIGR01073; pcrA; 1.
DR   PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF21196; PcrA_UvrD_tudor; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; DNA-binding {ECO:0000256|RuleBase:RU364053};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000002512}.
FT   DOMAIN          1..259
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          260..542
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         2..9
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   733 AA;  83461 MW;  82937BB0BD3EFAA5 CRC64;
     MAGAGSGKTR VLTHRIAYLI DEKFINPWNI LAITFTNKAA REMKERAFAL NAATQETLIA
     TFHSMCVRIL RRDADHIGYN RNFTIVDPGE QRTLMKRIFK NFNIDSKKWN ERAVLAAISN
     AKNDLLDEIA YENRAGDSYT QLVAKCYKAY QSELRQSEAM DFDDLIMLTL RLFDQNPDVL
     AYYQQRYQYI HVDEYQDTNH AQYQLVKLLA SRFKNICVVG DADQSIYGWR GADMQNILDF
     EKDYPEAKVV LLEENYRSSK KILQAANDVI KNNRNRRDKK LWTQNDDGEQ IVYYRADDEQ
     DEAVFVASTI ANIVREMGKN FKDFAVLYRT NAQSRTIEEA LLKSNIPYTM VGGTKFYSRK
     EIRDIIAYLN VIANTADNIS FERIVNEPKR GVGPGTLEKI RNFANLQGMS LLEASENIML
     SSIKGKAVQA VYELANMIID LRSKLDHYSI TEVVEAVLDS SGYLEVLEIQ KTLESQTRIE
     NIEEFLSVTK NFDDTTDDVP ENETGLERLS RFLNDLALIA DTDEAESESA EVTLMTLHAA
     KGLEFPIVFL IGLEEGVFPL SRSMEEESEL EEERRLAYVG ITRAEQMLFI TNANSRTLYG
     RTSYNRESRF IQEISEDLLV HQGLARPARA SFKVSYQDSN ETKFGQGMSL AQALQARKVA
     SQPKKSPFSN SKDDQKEHID WQIGDTAHHK KWGDGTVLEV SGSGSAQELK IKFPEIGLKK
     VLASVAPLEK KET
//
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