ID A0A0A0JJZ0_9MICO Unreviewed; 832 AA.
AC A0A0A0JJZ0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364053};
DE EC=5.6.2.4 {ECO:0000256|RuleBase:RU364053};
GN ORFNames=N803_05370 {ECO:0000313|EMBL:KGN36372.1};
OS Knoellia subterranea KCTC 19937.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Knoellia.
OX NCBI_TaxID=1385521 {ECO:0000313|EMBL:KGN36372.1, ECO:0000313|Proteomes:UP000030011};
RN [1] {ECO:0000313|EMBL:KGN36372.1, ECO:0000313|Proteomes:UP000030011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 19937 {ECO:0000313|EMBL:KGN36372.1,
RC ECO:0000313|Proteomes:UP000030011};
RA Zhu W., Wang G.;
RT "The genome sequence of Knoellia subterranea.";
RL Submitted (AUG-2013) 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}.
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:KGN36372.1}.
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DR EMBL; AVPK01000011; KGN36372.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0JJZ0; -.
DR STRING; 1385521.N803_05370; -.
DR eggNOG; COG0210; Bacteria.
DR Proteomes; UP000030011; 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:UP000030011}.
FT DOMAIN 77..376
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 377..663
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 98..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 832 AA; 91244 MW; 3C4DC946239A92D5 CRC64;
MDFGDALGAS GSGRSDTTPG ADTAPTTDHN THDSAHAAMV NAAGVPSWAV DGDAAVPSEP
AWGATAAPMI DPDALLEGLN EEQREAVLHA GSPLLIIAGA GSGKTRVLTH RIAHLLAARN
VQPGQILAIT FTNKAAAEMR ERVAQLVGPR AKAMWVMTFH SACVRILRRE ADKLGMKSTF
SIYDAADSQR LMAMVLRDMD LDPKRYNPRT FGHQVSNLKN ELIDEETYAG RVGGEPSAEN
PGGTHTERLL AQAYTAYQRR LRQANALDFD DIIMLTVHML QAFPDVAEHY RRRFRHIMVD
EYQDTNHAQY QLIRELVGHG DNRGEHSVEP SELVVVGDAD QSIYAFRGAT IRNIIEFEED
YPDARTILLE RNYRSTQTIL TAANAVIARN ETRRKKNLWT DSGSGAPIVG YVGDNEHDEA
SFVARSIDKL GDQHGVKPGD VAVFYRTNAQ SRALEEVFVR VGLPYKVVGG TRFYERREVK
DALAYLRVLS NPADSVNLRR ILNVPKRGIG DRAEAVVGAL AERERITFIE ALGRPEDAPG
IATRSVTSIK AFTALLEELG KVRDDDEAGV ADLLEAIIEQ SGYLAELRAS HDPQDETRIE
NLHELVAVAR EFDEARAETG EVNNLEDFLE QVSLVADADE IPDSAEAEEQ GVVTLMTLHT
AKGLEFPVVF LTGLEDGTFP HLRSLGDPKE LEEERRLAYV GITRARERLH LSRAAVRSAW
GAPQYNPPSR FLGEIPDDLV EWERELSGAA AVGHRGQRPA VASLAARPGV RSPGNRPIIP
LSPGDKVTHD TFGMGSVVRT MGEGDKTQAE VDFGGETGVK RFLLRFAPLE KL
//
