ID A5CFB9_ORITB Unreviewed; 716 AA.
AC A5CFB9;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
DE AltName: Full=DNA 3'-5' helicase II {ECO:0000256|ARBA:ARBA00034923};
GN Name=uvrD {ECO:0000313|EMBL:CAM81056.1};
GN OrderedLocusNames=OTBS_1961 {ECO:0000313|EMBL:CAM81056.1};
OS Orientia tsutsugamushi (strain Boryong) (Rickettsia tsutsugamushi).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Orientia.
OX NCBI_TaxID=357244 {ECO:0000313|EMBL:CAM81056.1, ECO:0000313|Proteomes:UP000001565};
RN [1] {ECO:0000313|EMBL:CAM81056.1, ECO:0000313|Proteomes:UP000001565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boryong {ECO:0000313|EMBL:CAM81056.1,
RC ECO:0000313|Proteomes:UP000001565};
RX PubMed=17483455; DOI=10.1073/pnas.0611553104;
RA Cho N.-H., Kim H.-R., Lee J.-H., Kim S.-Y., Kim J., Cha S., Kim S.-Y.,
RA Darby A.C., Fuxelius H.-H., Yin J., Kim J.H., Kim J., Lee S.J., Koh Y.-S.,
RA Jang W.-J., Park K.-H., Andersson S.G.E., Choi M.-S., Kim I.-S.;
RT "The Orientia tsutsugamushi genome reveals massive proliferation of
RT conjugative type IV secretion system and host-cell interaction genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7981-7986(2007).
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 -!- 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}.
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DR EMBL; AM494475; CAM81056.1; -; Genomic_DNA.
DR RefSeq; WP_011945122.1; NC_009488.1.
DR AlphaFoldDB; A5CFB9; -.
DR KEGG; ots:OTBS_1961; -.
DR eggNOG; COG0210; Bacteria.
DR HOGENOM; CLU_004585_5_10_5; -.
DR Proteomes; UP000001565; Chromosome.
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:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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; 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: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 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};
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:UP000001565}.
FT DOMAIN 6..281
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 282..552
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 716 AA; 81934 MW; 3164175DF0BDB2C8 CRC64;
MSQYLLDLNP EQREAVITTN GPLLVLAGAG TGKTRVITYR IAYIIDQFMA SPEEILAVTF
TNKAATEMQS RVAEITNNTT GIYIGTFHAI ATKILKAHAE LVGLTSSFSI IDQSEQVRVI
KNICETHGIS TKNYSPKDIC EIISRWKDLG EQPKIDCHTP IYQVAQKIYQ HYQTELQKSN
VVDFGDLLLY NMKIFSEYPD VLNFYQTKFK YVFIDEYQDT NNVQYFWAKA LVNLHENLCC
VGDDDQSIYS WRGANIENIL KFKDDFKNAK LIKLEQNYRS TNSILTAASS IICNNKYRHD
KKLWTNKQSD QPIRIVYCYN DREEARFISS EIKKLITKSP NLSIAVLVRS SSQAHVLEES
FFSNNIKYQV IGGFRFFDRM EIADMIAYLR VLVNHNDNLA LTRIINVPKR SIGPATLHTI
KEYAQQHESS MFTAIEQILS KKLLKPQLEL TLQSLINKFK EWHSLYKAGY TPAKVTEIIC
EDSNYLQMLK DDKSSQSDRR IENIQEMIRA MLDYNSIEEF LEHTSLFLER DNGINAKDNS
AVSLMTLHAS KGLEFDVVFL PGLEEGVFPH QKSLIAEDQR ALEEERRIAY VGITRAKQSL
YISYADQRRI FNEFVKLQPS RFLLDIPDSI SLSTTSMIHY SSAANNNYFQ KSLSAAMPNS
QSKASSKFFT GAKVLHKQFG QGTVIRIMND NIEVAFYVGG IKTIKQQFLT INARLG
//
