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Database: UniProt
Entry: A4FP72_SACEN
LinkDB: A4FP72_SACEN
Original site: A4FP72_SACEN 
ID   A4FP72_SACEN            Unreviewed;       873 AA.
AC   A4FP72;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   Name=uvrD {ECO:0000313|EMBL:CAM05847.1};
GN   OrderedLocusNames=SACE_6681 {ECO:0000313|EMBL:CAM05847.1};
GN   ORFNames=A8924_7034 {ECO:0000313|EMBL:PFG99489.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS   NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAM05847.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAM05847.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC   {ECO:0000313|EMBL:CAM05847.1};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA   Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
RN   [2] {ECO:0000313|EMBL:PFG99489.1, ECO:0000313|Proteomes:UP000225825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG99489.1,
RC   ECO:0000313|Proteomes:UP000225825};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (SEP-2017) 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   -!- 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; AM420293; CAM05847.1; -; Genomic_DNA.
DR   EMBL; PDBV01000001; PFG99489.1; -; Genomic_DNA.
DR   RefSeq; WP_009943395.1; NZ_PDBV01000001.1.
DR   AlphaFoldDB; A4FP72; -.
DR   STRING; 405948.SACE_6681; -.
DR   KEGG; sen:SACE_6681; -.
DR   eggNOG; COG0210; Bacteria.
DR   HOGENOM; CLU_004585_5_2_11; -.
DR   OrthoDB; 9806690at2; -.
DR   Proteomes; UP000006728; Chromosome.
DR   Proteomes; UP000225825; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
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; 3.
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; 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};
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:UP000006728}.
FT   DOMAIN          32..333
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          334..687
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          263..288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          570..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          777..808
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         53..60
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   873 AA;  95429 MW;  282808E08B600857 CRC64;
     MSTLFDLPQD GSSGPAETPS QRRGPDPQDL LAGLNPQQRD AVEHSGSPLL VVAGAGSGKT
     RVLTNRIAYL LARGVHPGQI MAITFTNKAA AEMKERVADL VGRRANAMWV STFHSMCVRV
     LRREAKTLGM SSNFSIYDAD DSRRLITIIA RELELDSKRY PARTLAVHIS NLKNELLTPE
     DAAERAGNDV ERKVAQVYTA YQRRLAESNA MDFDDLIMRT VELLQGYPAV AEHYRRRFRH
     VLVDEYQDTN HAQYVLVREL VGTNRPGEPD ADSEADADES GEETVEPGEL CVVGDADQSI
     YAFRGATIRN IEEFERDYPE ARAILLEQNY RSTQTILSAA NAVIRRNPNR RDKRLWSDAG
     DGEQIVGYVG DNEHDEAAFV AGEIDRLVDE GEATFNDIAV FYRTNNQSRV FEEVFIRLGL
     PYRVVGGVRF YERREVRDAL AYLRVLDNPE DTVSLRRILN VPKRGIGDRA EAVVAAHAEQ
     ERISFAAALR KAAAGEVPLL NTRSQRAIAG FVEMLDELHG IAAESDVADV LEAVLDRTGY
     RAELEDSDDP QDATRVENLT ELVTVAREFI EARSPEPAAA PGDNAEDLDD AAGDLGENTS
     DLGNSAEDAA APGDGATGDE DAHASAEAVV APAEPAAEDD DEAALGLPAD DSLSAFLERV
     SLVADADSLP DSGDGVVTLM TLHTAKGLEF PVVFCTGWED GIFPHMRALG EPAELAEERR
     LAYVGITRAR QRLYLSRALM RSAWGQPMTN PASRFLTEIP DELVHWRRIE PERAAPQVRS
     TWGRRNSGFD RGGSDSAQAG LAERGMRSTP AKGWKDAVAI KLDAGDRVTH DKYGLGTVIA
     TEGEGPRATA TIDFGSSGTV RLMLIGSVPL TKL
//
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