ID   UVRD_RICCN              Reviewed;         653 AA.
AC   Q92HZ6;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Probable DNA helicase II homolog;
DE            EC=3.6.4.12;
GN   Name=uvrD; OrderedLocusNames=RC0624;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
CC   -!- FUNCTION: Has both ATPase and helicase activities. Unwinds DNA duplexes
CC       with 3' to 5' polarity with respect to the bound strand and initiates
CC       unwinding most effectively when a single-stranded region is present.
CC       Involved in the post-incision events of nucleotide excision repair and
CC       methyl-directed mismatch repair (By similarity). {ECO:0000250}.
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=3.6.4.12;
CC   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE006914; AAL03162.1; -; Genomic_DNA.
DR   PIR; H97777; H97777.
DR   RefSeq; WP_010977253.1; NC_003103.1.
DR   AlphaFoldDB; Q92HZ6; -.
DR   SMR; Q92HZ6; -.
DR   EnsemblBacteria; AAL03162; AAL03162; RC0624.
DR   KEGG; rco:RC0624; -.
DR   PATRIC; fig|272944.4.peg.710; -.
DR   HOGENOM; CLU_004585_5_10_5; -.
DR   OMA; YQDTNRT; -.
DR   Proteomes; UP000000816; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:UniProtKB-EC.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:InterPro.
DR   Gene3D; 1.10.10.160; -; 1.
DR   Gene3D; 3.40.50.300; -; 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   PANTHER; PTHR11070; PTHR11070; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01073; pcrA; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA repair; DNA replication; DNA-binding;
KW   Helicase; Hydrolase; Nucleotide-binding.
FT   CHAIN           1..653
FT                   /note="Probable DNA helicase II homolog"
FT                   /id="PRO_0000286459"
FT   DOMAIN          8..288
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT   DOMAIN          289..559
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00617"
FT   BINDING         32..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT   BINDING         286
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   653 AA;  75051 MW;  CF533C14DBA33A1C CRC64;
     MQNQDFIHTL NPEQQKAVLH TEGPLLLLAG AGTGKTKVLT SRIANIIHQN LASPQNILAV
     TFTNKAAKEM AERVNSLINC YGLNIGTFHS MAARILRDQI EHLNLGLNNR FTIISHDDQL
     KLVKDIVKLK DIDTKKYAPK LIHIIISRWK DQGLLPTKLS VSDTNLPLQR VAKLVYEEYQ
     KNLLISNVLD FGDLLLYNNE LFIKNSEILR YYQEKYRYIL IDEYQDTNVV QYLWARMLAS
     LYKNICCVGD DDQSIYGWRG AEVGNILRFE KDFAGATIIK LEQNYRSTLP ILAAASNVIN
     NNKNRHGKTL WTDRENGEKI KIISCWSDKE EARYIAGEID KLVRENRYNA GNIAILVRAG
     FQTRSFEEAF INSAMPYKII GGLRFYERME IRDVLAYIRI SLNQNDNLAL ERIINVPKRA
     IGAASLNKIR GYALERNISN FAAIKEMLEI GEIKAKSYET LKDLVTKIDN WYERFSIDAP
     INVVKAILDD SGYLEMLQEE KTEEAFGRIE NINEMLRAIA EFNDVHDFIE HSSLVMENEV
     LETNYGGSVT IMTLHAAKGL EFDVVFLPGW EEGVFPSQRS LDEEGEKGLE EERRIAYVGI
     TRAKKDLYIT HAESRKIFYE IVRSYPSRFI TEIPDEITIR TSSMKKYNSF YKF