ID A0A1L7FFM9_9PSEU Unreviewed; 829 AA.
AC A0A1L7FFM9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364053};
DE EC=5.6.2.4 {ECO:0000256|RuleBase:RU364053};
GN ORFNames=UA75_28295 {ECO:0000313|EMBL:APU23630.1};
OS Actinoalloteichus sp. GBA129-24.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinoalloteichus.
OX NCBI_TaxID=1612551 {ECO:0000313|EMBL:APU23630.1, ECO:0000313|Proteomes:UP000185506};
RN [1] {ECO:0000313|EMBL:APU23630.1, ECO:0000313|Proteomes:UP000185506}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GBA129-24 {ECO:0000313|EMBL:APU23630.1,
RC ECO:0000313|Proteomes:UP000185506};
RA Ruckert C., Nouioui I., Willmese J., van Wezel G., Klenk H.-P.,
RA Kalinowski J., Zotchev S.B.;
RT "Complete genome sequence of Actinoalloteichus fjordicus DSM 46856
RT (=GBA129-24).";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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 ECO:0000256|RuleBase:RU364053};
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, ECO:0000256|RuleBase:RU364053}.
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DR EMBL; CP016077; APU23630.1; -; Genomic_DNA.
DR RefSeq; WP_075742858.1; NZ_CP016077.1.
DR AlphaFoldDB; A0A1L7FFM9; -.
DR STRING; 1612551.UA75_28295; -.
DR KEGG; acti:UA75_28295; -.
DR OrthoDB; 9806690at2; -.
DR Proteomes; UP000185506; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:InterPro.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR CDD; cd18807; SF1_C_UvrD; 2.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR01073; pcrA; 1.
DR PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF21196; PcrA_UvrD_tudor; 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}; DNA-binding {ECO:0000256|RuleBase:RU364053};
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}.
FT DOMAIN 28..328
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 329..640
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 576..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 49..56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 829 AA; 90151 MW; 04A2D72315F06997 CRC64;
MNTLFELSPD ASTSAPARRA VDSAALLAGL NPQQHQAVTH QGSPLLVVAG AGSGKTRVLT
SRIGYLLAER DVHPGQILAI TFTNKAAAEM KERVADLVGP RANLMWVSTF HSMCARLLRR
EARTLRELLA GDDSAGTANS NFSIYDGDDA KRLITQVARD LELDPKRFPA RTLAVHISNL
KNELIGPVEA AEQAADELQR RVAQVYAAYQ RRLHSSNALD FDDLILRSVE LLQRFPDVAG
YYRRRFRHVM VDEYQDTNHA QYVLVRELVG AATGDQGPAV PPAELCVVGD ADQSIYAFRG
ATIRNIVEFE RDYPDARTIM LEQNYRSTQT ILSAANAVIS RNPDRRDKRL WTDSGEGEKI
VGYVADNEHD EAAFVAREID RLVDAGEVVN GDIAVFYRTN NQSRVFEEIF IRLGLPYRVV
GGVRFYERRE VRDALAYLRA LANPDDAVGL RRILNTPKRG IGDRAEAVIS VYAEQQEIGF
APALRAAAEG RVALLNSRSQ KAVAGFVALM DELRAELDAG HDVAEILEAV LERTGYRATL
EDSDDPQDAS RLENLTELVT VAREFVAQAL AVENEAAPVS QETAEPLSTS TDADADAEDG
PPAGSLAAFL ERVALVADSD SVPESEDGVV TLMTLHTAKG LEFPVVFCTG WEDGIFPHLR
ALGDPAEAAE ERRLAYVGIT RARERLYLSR ALVRSAWGQP MTNPASRFLE EIPTDLIDWR
RLAPDRSAPS VATRWGGRSG SGFGSDSAQA AVAQGGMKTT GFGGFGRGGA ANAVPMKLDV
GDRVSHDKYG LGKVVATDGS GPRTTATIDF GTAGRVKLML IGSVPMTKL
//