ID A0A0W1L3H8_9GAMM Unreviewed; 672 AA.
AC A0A0W1L3H8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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 ORFNames=ATS75_13045 {ECO:0000313|EMBL:KTF14171.1};
OS Pseudoalteromonas sp. H105.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1348393 {ECO:0000313|EMBL:KTF14171.1, ECO:0000313|Proteomes:UP000054685};
RN [1] {ECO:0000313|EMBL:KTF14171.1, ECO:0000313|Proteomes:UP000054685}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H105 {ECO:0000313|EMBL:KTF14171.1,
RC ECO:0000313|Proteomes:UP000054685};
RA Duhaime M.B., Sullivan M.B., Wichels A.;
RT "Six Pseudoalteromonas strains isolated from surface waters of Kabeltonne
RT offshore Helgoland, North Sea.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KTF14171.1}.
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DR EMBL; LOFH01000007; KTF14171.1; -; Genomic_DNA.
DR RefSeq; WP_058560982.1; NZ_LOFH01000007.1.
DR AlphaFoldDB; A0A0W1L3H8; -.
DR STRING; 1348393.ATS75_13045; -.
DR OrthoDB; 9806690at2; -.
DR Proteomes; UP000054685; Unassembled WGS sequence.
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 NCBIfam; TIGR01074; rep; 1.
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}.
FT DOMAIN 1..280
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 281..563
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 22..29
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 672 AA; 77043 MW; DE5F153343ADA5A4 CRC64;
MKLNPKQDEA VKYISGPCLV LAGAGSGKTR VITNKIAYLV QKCEYQARNI AAVTFTNKAA
KEMRERVMQT LGKQESKGLW VSTFHTLGLE IIKKELSTLG FKPGFSLFDD QDTNQLLGDL
TEDELKKDKD LLNLLKMQIG SWKNELILPE QAIREAREPQ KALFAQLYAR YQTQLRAYNA
LDFDDLIMIP TLLLTNNATS RERWQQRFRY LLVDEYQDTN TSQYQLVKLL VGERARFTVV
GDDDQSIYSW RGARPQNLVL LSKDFPGLRL IKLEQNYRSA GRILKAANIL IANNPHEFDK
KLFSELGYGE PIKVIGCRDE EHESERVVAE IISHKFMKRT SYKDYAILYR GNHQARGFEK
SLMSNRIPYK ISGGMSFFSR SEIKDIMAYL RLLVNQDDDN AFLRIVNTPR REIGTVTLEK
LGTLANEKHA SLFATCFDND LSYRLKGRGL NSLAGFARWV VELSDNAVRG DTLEAVKDLI
RQINYEAYLY ESSPSAKAAE MRMKNVSELY RWITDMLTGD ADNQPMTLAE VVSKLTLRDM
LERNEEEDES DAVQLLTLHA SKGLEYPYVF MVGMEEGLLP HQVSIDEENV DEERRLAYVG
ITRAQQELTM TYAKIRRQFG ETSQTELSRF VQELPQDDLA FENRKAPNTQ AERMEKGQAR
VANLRAMLKK PN
//
