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Database: UniProt
Entry: T1ZDX9_STRIT
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Original site: T1ZDX9_STRIT 
ID   T1ZDX9_STRIT            Unreviewed;       760 AA.
AC   T1ZDX9;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 52.
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:AGU75911.1};
GN   ORFNames=SIR_0539 {ECO:0000313|EMBL:AGU75911.1};
OS   Streptococcus intermedius B196.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus; Streptococcus anginosus group.
OX   NCBI_TaxID=862967 {ECO:0000313|EMBL:AGU75911.1, ECO:0000313|Proteomes:UP000016233};
RN   [1] {ECO:0000313|EMBL:AGU75911.1, ECO:0000313|Proteomes:UP000016233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B196 {ECO:0000313|EMBL:AGU75911.1,
RC   ECO:0000313|Proteomes:UP000016233};
RX   PubMed=24341328; DOI=10.1186/1471-2164-14-895;
RA   Olson A.B., Kent H., Sibley C.D., Grinwis M.E., Mabon P., Ouellette C.,
RA   Tyson S., Graham M., Tyler S.D., Van Domselaar G., Surette M.G.,
RA   Corbett C.R.;
RT   "Phylogenetic relationship and virulence inference of Streptococcus
RT   Anginosus Group: curated annotation and whole-genome comparative analysis
RT   support distinct species designation.";
RL   BMC Genomics 14:895-895(2013).
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; CP003857; AGU75911.1; -; Genomic_DNA.
DR   RefSeq; WP_021002567.1; NC_022246.1.
DR   AlphaFoldDB; T1ZDX9; -.
DR   KEGG; sib:SIR_0539; -.
DR   PATRIC; fig|862967.3.peg.530; -.
DR   eggNOG; COG0210; Bacteria.
DR   HOGENOM; CLU_004585_5_2_9; -.
DR   OrthoDB; 9810135at2; -.
DR   Proteomes; UP000016233; 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   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:UP000016233}.
FT   DOMAIN          6..284
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          285..566
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         27..34
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   760 AA;  86085 MW;  1E00466206F5C3E9 CRC64;
     MNPLLTGMND RQAEAVQTTD GPLLIMAGAG SGKTRVLTHR IAYLIDEKLV NPWNILAITF
     TNKAAREMKE RAFSLNPATE DCLIATFHSM CVRILRREAD HIGYNRNFTI VDPGEQRTLM
     KRILKNLNLD PKKWNERAIL GTISNAKNDL IDEVAYENMA GDMYTEIVAK CYTAYQKELR
     QSEAMDFDDL IMLTLRLFDQ NPDVLTYYQQ RYQYIHVDEY QDTNHAQYQL VKLLASRFKN
     ICVVGDADQS IYGWRGADMQ NILDFEKDYP EAKVVLLEEN YRSTKTILQA ANEVIRNNRN
     RRPKNLWTQN EDGEEIVYYR ANDEQDEALF VARTIDQLTR EGYSHKDFAV LYRTNAQSRT
     VEEALLKANI PYTMVGGTKF YSRKEIRDVI SYLNLIANPS DNISYERVVN EPKRGVGPGT
     VEKIRNFAAS QNVSLLEASS QIMLSLVKGK AAQSVFDFAN LILNLRERLD ELTVTELVEI
     VLEKTGYTEQ LVAQGTLESQ ARIENIEEFL SVTKNFDEYS ENDTEETGLD KLSRFLNDLA
     LVADTDDAGT QESSEVTLMT LHAVKGLEFP VVFIIGMEEN VFPLSRATEE EDELEEERRL
     AYVGITRAEK VLFLTNANSR LLYGKTNYNR PTRFLNEISS DLLNYQGLAR PANTSFKASY
     VNGKTVQFGQ GTSLAQALQE RKRQVGPSSI SSSQLPFGKN IEATQPDLNW AIGDIAHHKK
     WGDGTVLEVS GSGSSLELKI NFPEVGLKKL LASVAPIEKK
//
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