ID   A0A014M6K5_9GAMM        Unreviewed;       683 AA.
AC   A0A014M6K5;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   Name=helD {ECO:0000313|EMBL:EXU73679.1};
GN   ORFNames=BG55_20885 {ECO:0000313|EMBL:EXU73679.1};
OS   Erwinia mallotivora.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=69222 {ECO:0000313|EMBL:EXU73679.1, ECO:0000313|Proteomes:UP000019918};
RN   [1] {ECO:0000313|EMBL:EXU73679.1, ECO:0000313|Proteomes:UP000019918}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BT-MARDI {ECO:0000313|EMBL:EXU73679.1,
RC   ECO:0000313|Proteomes:UP000019918};
RA   Redzuan R., Abu Bakar N., Badrun R., Mohd Raih M.F., Rozano L.,
RA   Mat Amin N.;
RT   "Draft genome of Erwinia mallotivora strain BT-MARDI, a papaya dieback
RT   pathogen.";
RL   Submitted (FEB-2014) 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   -!- 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:EXU73679.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JFHN01000074; EXU73679.1; -; Genomic_DNA.
DR   RefSeq; WP_034941074.1; NZ_JFHN01000074.1.
DR   AlphaFoldDB; A0A014M6K5; -.
DR   STRING; 69222.BG55_20885; -.
DR   PATRIC; fig|69222.5.peg.4265; -.
DR   OrthoDB; 5298826at2; -.
DR   Proteomes; UP000019918; Unassembled WGS sequence.
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:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   CDD; cd17932; DEXQc_UvrD; 1.
DR   CDD; cd18807; SF1_C_UvrD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR022161; Helicase_IV_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070:SF63; DNA HELICASE IV; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF12462; Helicase_IV_N; 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.
PE   4: Predicted;
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:UP000019918}.
FT   DOMAIN          195..504
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   BINDING         216..223
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   683 AA;  78317 MW;  4D81FDF7DE986325 CRC64;
     MELKATSLGK HLAQHPYNRV RLLSAGIEVS GEKHEYLIPF NQLLAIRCKR GLVWGELEFT
     LPDEKVVRLH GTEWQETQRF FHYLNQSWQS WSTEMSNISA QVLNDAVTRI KHLEQQDKWL
     KRSDIAEWDQ AVLQAFASLP LPVARLPEFT NCRDAYQFLQ QWLENGDGRR KERNTQWSQK
     MLQQYADYFN TVETSPLNTS QARAVINGEE AVLVLAGAGS GKTSVLVARV GWLLTRRQAT
     PDQILLLAFG RKAAEEMNDR ITARLDTEGI QARTFHSLAL HIIQQGSTKS PKISKLETDS
     KLRQQLLIDI WRQQCSEKKA HANGWRQWLE GDLDWQPGED FWNDERLAKR LVSRLEQWLG
     LMRMHGGAQA AMIESAPEDM REQFAKRVKL MAPIMKAWKR ELKEEGAVDF SGLIHQAINI
     LDKGRFITPW KHILVDEFQD ISPQRAALLA ALRRQNKQTS LFAVGDDWQA IYRFSGAEMT
     LTTAFHHHFG EGESCILDTT YRFNDRIGEI ASNFIQSNPY QLKKPLNSVS KGNKKSVLLL
     PEAQLEALLD KLSGYVTPDE RILVLTRYHY LRPHLLEKAV TRWPKLKIDH ATIHASKGQQ
     ADYVLLLGLK AGSDGFPAVA RESVMEKALL PQPEDFMDAE ERRLAYVAIT RARKQVWMLF
     DADAPSVFVE EFKRLGVPVL RKP
//