ID D6KBS8_9ACTN Unreviewed; 841 AA.
AC D6KBS8;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364053};
DE EC=5.6.2.4 {ECO:0000256|RuleBase:RU364053};
GN ORFNames=SSTG_02997 {ECO:0000313|EMBL:EFF92678.2};
OS Streptomyces sp. e14.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=645465 {ECO:0000313|EMBL:EFF92678.2, ECO:0000313|Proteomes:UP000004704};
RN [1] {ECO:0000313|EMBL:EFF92678.2, ECO:0000313|Proteomes:UP000004704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=e14 {ECO:0000313|Proteomes:UP000004704};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Streptomyces sp. strain e14.";
RL Submitted (OCT-2009) 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; GG753626; EFF92678.2; -; Genomic_DNA.
DR RefSeq; WP_009190225.1; NZ_GG753626.1.
DR AlphaFoldDB; D6KBS8; -.
DR STRING; 645465.SSTG_02997; -.
DR eggNOG; COG0210; Bacteria.
DR OrthoDB; 4812256at2; -.
DR Proteomes; UP000004704; Unassembled WGS sequence.
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:UP000004704}.
FT DOMAIN 86..380
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 381..663
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 107..114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 841 AA; 92606 MW; 82E941ACA9A5F416 CRC64;
MSSLFDDSFL ADLQAPRAHG EEPPPPPEDD HAPEPVPDDL FGGKFDVPPD PESYLPDPRD
SDGYGRDAYY RDGAPRPVID SAALLEGLNN NQRAAVVHAG SPLLIVAGAG SGKTRVLTHR
IAYLLAERGV HPGQILAITF TNKAAGEMKE RVEHLVGPRA NAMWVMTFHS ACVRILRRES
KRLGFTSSFS IYDAADSKRL MALVCRDLDL DPKRYPPKSF SAKISNLKNE LIDEEDFAAQ
ATDGFEKTLA QAYALYQSRL REANALDFDD LIMTTVNLLR AFPDVAEHYR RRFRHVLVDE
YQDTNHAQYA LVRELVGTAE HPVDVPPSEA DVPPAELCVV GDADQSIYAF RGATIRNILQ
FEEDYPDATT ILLEQNYRST QTILSAANAV IERNESRRPK NLWTNAGAGA RITGYVADTE
HDEAQFVADE IDRLTDAGEA KAGDVAVFYR TNAQSRVFEE IFIRVGLPYK VVGGVRFYER
KEVRDVLAYL RVLANPEDSV PLRRILNVPK RGIGERAEAM VDALAQREKI SFPQALRRVD
EAYGMAARSA NAVKRFNTLM EELRTIVESG AGPATILEAV LERTGYLAEL QSSTDPQDET
RIENLQELAA VALEFEQERG EGEPVALSEF LEQVALVADS DQIPDEEDGD GVITLMTLHT
AKGLEFPVVF LTGMEDGVFP HMRALGQVKE LEEERRLAYV GITRARERLY LTRSAMRSAW
GQPSYNPPSR FLEEIPQTHV DWKRTGGSVA APSGPASGVA ASLSSSRSRS SASGASGFAT
RRTPDKPVVS LAVGDRVTHD QFGLGTVVAV KGTGGNAEAT IDFGDAKPKR LLLRYAPVEK
L
//
