UVRD_RICPR
ID UVRD_RICPR Reviewed; 658 AA.
AC Q9ZD95;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Probable DNA helicase II homolog;
DE EC=3.6.4.12;
GN Name=uvrD; OrderedLocusNames=RP447;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
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; AJ235271; CAA14904.1; -; Genomic_DNA.
DR PIR; F71703; F71703.
DR RefSeq; NP_220828.1; NC_000963.1.
DR RefSeq; WP_004599479.1; NC_000963.1.
DR AlphaFoldDB; Q9ZD95; -.
DR SMR; Q9ZD95; -.
DR STRING; 272947.RP447; -.
DR EnsemblBacteria; CAA14904; CAA14904; CAA14904.
DR GeneID; 57569572; -.
DR KEGG; rpr:RP447; -.
DR PATRIC; fig|272947.5.peg.460; -.
DR eggNOG; COG0210; Bacteria.
DR HOGENOM; CLU_004585_5_2_5; -.
DR OMA; YQDTNRT; -.
DR Proteomes; UP000002480; 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; Reference proteome.
FT CHAIN 1..658
FT /note="Probable DNA helicase II homolog"
FT /id="PRO_0000102081"
FT DOMAIN 12..293
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT DOMAIN 294..564
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00617"
FT BINDING 36..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT BINDING 291
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 658 AA; 75389 MW; CCFA97690F0E0BDC CRC64;
MKDKIQNQNF MHTLNAEQKK AALHTEGPLL LLAGAGTGKT KVLTSRIANI IHQNLALPHN
ILAVTFTNKA AKEMSERVHN LINCYGLNIG TFHSMAAKIL RDQIENLNLG FNNRFTIISH
DDQLTLVKDI VKLKKDIDAK KYTPKLIHII ISRWKDQGLL PNKLSTSDTN LPLQKIAKLV
YEEYQKNLLI SNVLDFGDLL LYNNELFIKN PAVLKYYQEK YRYILIDEYQ DTNIAQYLWA
RMLASLYRNI CCVGDDDQSI YGWRGAEVGN ILRFEKDFAG ATIIKLEQNY RSTLPILAAA
SNVINNNKNR HSKTLWTDSS SGEKIKIISC LSDKEEARYI ACEIDKLVKE ERYNAGNIAI
LVRAGFQTRS FEEAFINSAI PYKIIGGLRF YERMEIRDVL AYIRISLNQN DNLALERIIN
VPKRAIGAAS LNKIRSYALE RNISNFAAIK EILEIGNIKA KSYESLKDLL TKIDNWYEQF
IIDTPINVVK AILDDSGYLA MLKEEKTEEA FGRIENINEM LRAIAEFNDI HDFIEYSSLV
MENEVLETNY GGSVTIMTLH AAKGLEFDVV FLPGWEEGVF PSQRSLDEDG EKGLEEERRI
AYVGITRAKK DLYITHAESR KIFYEIVRSC PSRFINEIPD EITIRTSSMK QYNSFYKF