ID D3HNV7_LEGLN Unreviewed; 667 AA.
AC D3HNV7;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=ATP-dependent DNA helicase Rep {ECO:0000256|HAMAP-Rule:MF_01920};
DE EC=5.6.2.4 {ECO:0000256|HAMAP-Rule:MF_01920};
DE AltName: Full=DNA 3'-5' helicase Rep {ECO:0000256|HAMAP-Rule:MF_01920};
GN Name=rep {ECO:0000256|HAMAP-Rule:MF_01920,
GN ECO:0000313|EMBL:CBJ10570.1};
GN OrderedLocusNames=LLO_0242 {ECO:0000313|EMBL:CBJ10570.1};
OS Legionella longbeachae serogroup 1 (strain NSW150).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=661367 {ECO:0000313|EMBL:CBJ10570.1, ECO:0000313|Proteomes:UP000001060};
RN [1] {ECO:0000313|EMBL:CBJ10570.1, ECO:0000313|Proteomes:UP000001060}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSW150 {ECO:0000313|EMBL:CBJ10570.1,
RC ECO:0000313|Proteomes:UP000001060};
RX PubMed=20174605; DOI=10.1371/journal.pgen.1000851;
RA Cazalet C., Gomez-Valero L., Rusniok C., Lomma M., Dervins-Ravault D.,
RA Newton H., Sansom F., Jarraud S., Zidane N., Ma L., Bouchier C.,
RA Etienne J., Hartland E., Buchrieser C.;
RT "Analysis of the Legionella longbeachae genome and transcriptome uncovers
RT unique strategies to cause Legionnaires' disease.";
RL PLoS Genet. 6:E1000851-E1000851(2010).
CC -!- FUNCTION: Rep helicase is a single-stranded DNA-dependent ATPase
CC involved in DNA replication; it can initiate unwinding at a nick in the
CC DNA. It binds to the single-stranded DNA and acts in a progressive
CC fashion along the DNA in the 3' to 5' direction. {ECO:0000256|HAMAP-
CC Rule:MF_01920}.
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, ECO:0000256|HAMAP-
CC Rule:MF_01920};
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|HAMAP-Rule:MF_01920};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01920}.
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922, ECO:0000256|HAMAP-Rule:MF_01920}.
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DR EMBL; FN650140; CBJ10570.1; -; Genomic_DNA.
DR RefSeq; WP_003633421.1; NC_013861.1.
DR AlphaFoldDB; D3HNV7; -.
DR STRING; 661367.LLO_0242; -.
DR KEGG; llo:LLO_0242; -.
DR eggNOG; COG0210; Bacteria.
DR HOGENOM; CLU_004585_5_2_6; -.
DR OrthoDB; 9806690at2; -.
DR Proteomes; UP000001060; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-UniRule.
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 HAMAP; MF_01920; Helicase_Rep; 1.
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; IPR005752; Helicase_Rep.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF64; ATP-DEPENDENT DNA HELICASE REP; 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|HAMAP-
KW Rule:MF_01920};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_01920}; DNA-binding {ECO:0000256|HAMAP-Rule:MF_01920};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01920};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01920};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01920};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01920}; Reference proteome {ECO:0000313|Proteomes:UP000001060}.
FT DOMAIN 1..280
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 281..559
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 21..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
FT BINDING 278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01920"
SQ SEQUENCE 667 AA; 76027 MW; 1E0AB14E00E18CAB CRC64;
MLNSQQMAAV RHIDGPLLVL AGAGSGKTRV ITQKIAYLIN TCGYAANTVC AVTFTNKAAN
EMRARVAAVL PPATRRGLKV ATFHTLGLSI IKRHLDLCDL KKGFSIFDSE DCVQILRGFL
PANRATEKEF ILQIQQKISR WKNDLLTPDQ VINNPADAPY YEEAALLYPR YQQALKAYNA
VDFDDLIRLP VSLLSEHSSV STYWQNKIRH LLVDEYQDSN TSQYLLVKQL TGIRAHFTVV
GDDDQSIYAW RGAKPENLKQ LQLDYPQIKI IKLEQNYRST NIILHSANHL IANNQHLFEK
KLWSEFGHGE LLRVIRCKDE NDEAEQVVTD LISHKIRART EYGDYAILYR GNHQSRIFEK
VLRHYGIPYN ISGGQSWFAK AEVKDVFAYL KLLCNASDDA AFLRVINTPK RGIGETSLDA
LGHYAQNKGI SLYAASDHLA LGEYLAEKPR AALLTFKSWM EQIKVRVTTG SIVEHLKQMV
EDSGYEAHVY ELCDTPAKAQ KKMDNVWELL EWIERLLSKN KEQTLAEVIN KLILIDILDQ
ADEQVTDTLQ LMTLHASKGL EFPYVYLVGM EEELLPHRVS IDEDQIEEER RLAYVGITRA
QKGLCFTLAK QRRRAGELQD CLPSRFLDEL PPEHLEWFGK NVERSEEQSK HLAKTHLAGL
KSLLLER
//
