ID A0A0U4B7A7_9ACTN Unreviewed; 771 AA.
AC A0A0U4B7A7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364053};
DE EC=5.6.2.4 {ECO:0000256|RuleBase:RU364053};
GN ORFNames=AERYTH_03855 {ECO:0000313|EMBL:ALX03897.1};
OS Aeromicrobium erythreum.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=2041 {ECO:0000313|EMBL:ALX03897.1, ECO:0000313|Proteomes:UP000067689};
RN [1] {ECO:0000313|EMBL:ALX03897.1, ECO:0000313|Proteomes:UP000067689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR18 {ECO:0000313|EMBL:ALX03897.1,
RC ECO:0000313|Proteomes:UP000067689};
RX PubMed=1883712;
RA Miller E.S., Woese C.R., Brenner S.;
RT "Description of the erythromycin-producing bacterium Arthrobacter sp.
RT strain NRRL B-3381 as Aeromicrobium erythreum gen. nov., sp. nov.";
RL Int. J. Syst. Bacteriol. 41:363-368(1991).
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; CP011502; ALX03897.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U4B7A7; -.
DR STRING; 2041.AERYTH_03855; -.
DR KEGG; aer:AERYTH_03855; -.
DR PATRIC; fig|2041.4.peg.805; -.
DR Proteomes; UP000067689; 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; 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000067689}.
FT DOMAIN 17..300
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 301..593
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 680..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 771 AA; 84701 MW; FEBDA4ABDE7C3483 CRC64;
MAAARTRRAA RSETLLEGLN DAQRAAVSHE PGPVLVVAGA GSGKTRVLTR RIAWLISARG
AHPGSILAIT FTNKAAAEMR ERVAELVGGP SRAMWVSTFH SSCVRILRRE ANRFGYTSTF
SIYDAADSRR LMTLVCKDMG LDPKQVNPRA VLHWVSNLKN ELVDHESAGG RATNGTEELY
AEAYRLYQQR LRAANAMDFD DLIMQTVHLF QAFPEVRETY RRRFRHVLVD EYQDTNHAQY
ALVRELCDPE TDPDLDLMVV GDSDQSIYAF RGANIRNILE FEQDYPAAST VLLEQNYRST
QTILNAANAV ISRNEGRKDK KLWSAAGDGE RVVGYVGDDE RDEAQFIADE VDRLTDAGDA
KPSDVAIFYR TNAQSRVFEE VFIRVGLPYR VVGGVRFYER KEIKDALAYV RALVNPRDAV
SLRRIVNEPK RGIGDGAQAA VERFAAREQI SFWDALQRAE ETGDLAPRSL KAVQAFAATM
AELRELALSG EPADVVLEAA LTRSGYLSAL EDSKDPQDET RVENLAELVA VAREYVVNAS
TVSDEESGRE EADLTSGSLE AFLEQVALVA DADSIPDEGD GMVTLMTLHT AKGLEFPVVF
LTGLEDGVFP HLRALGDATE LQEERRLAYV GITRARERLY VTRAMSRAAW GAPSYNPASR
FLDEIPAHLL DWRREGQSPT AWTRAPSIGG GGSSSGGGRG QAFTAKAAAA RSQRKRAVPS
LTPGDRVTHD SFGLGTVVAL DGQGDNAVAS VDFGSQGVKR LLLRYAPVEK L
//
