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Database: UniProt
Entry: A0A2G0QB15_9GAMM
LinkDB: A0A2G0QB15_9GAMM
Original site: A0A2G0QB15_9GAMM 
ID   A0A2G0QB15_9GAMM        Unreviewed;       684 AA.
AC   A0A2G0QB15;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=Xhom_01898 {ECO:0000313|EMBL:PHM56410.1};
OS   Xenorhabdus hominickii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=351679 {ECO:0000313|EMBL:PHM56410.1, ECO:0000313|Proteomes:UP000225433};
RN   [1] {ECO:0000313|EMBL:PHM56410.1, ECO:0000313|Proteomes:UP000225433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17903 {ECO:0000313|EMBL:PHM56410.1,
RC   ECO:0000313|Proteomes:UP000225433};
RX   PubMed=28993611; DOI=10.1038/s41564-017-0039-9;
RA   Tobias N.J., Wolff H., Djahanschiri B., Grundmann F., Kronenwerth M.,
RA   Shi Y.M., Simonyi S., Grun P., Shapiro-Ilan D., Pidot S.J., Stinear T.P.,
RA   Ebersberger I., Bode H.B.;
RT   "Natural product diversity associated with the nematode symbionts
RT   Photorhabdus and Xenorhabdus.";
RL   Nat. Microbiol. 2:1676-1685(2017).
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   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000256|ARBA:ARBA00009922}.
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:PHM56410.1}.
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DR   EMBL; NJAI01000002; PHM56410.1; -; Genomic_DNA.
DR   RefSeq; WP_069316350.1; NZ_NJAI01000002.1.
DR   AlphaFoldDB; A0A2G0QB15; -.
DR   STRING; 351679.A9255_08630; -.
DR   KEGG; xho:A9255_08630; -.
DR   OrthoDB; 5298826at2; -.
DR   Proteomes; UP000225433; 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; 1.10.10.160; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; 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   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}.
FT   DOMAIN          195..505
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   684 AA;  78766 MW;  9C776604C89B1EAE CRC64;
     MELKSTQIGQ CLAQHPYNRV RLLNAGIEVS GDKHQYLIPF NQLLGIQCKR GIVWGELEFE
     LLEGKVVRLH GTEWQQTQHF YHHLLKEWQK WSLDMSDVSA DALAAQMNEI DKVKQQKRWI
     NAADLASLQQ QIQETFQSLP LPLQRITQFE NCRDDYQICL NWLDEGEKTV QTTNQQWIDH
     MLVQYEEFFR TVEISPLNRT QCRAVINGEK NILVLAGAGS GKTSVLVARA GWLLLRQQAL
     PEQVLLLAFG RQAADEMNER IQARLGTKAI KAKTFHALAL HIIQQGSNKE PKISELETDV
     QKRRDFLIQE WQKQCGEKKA QAKGWREWLT EELDWQLSEG EYWHDKQLAL RLSVRLERWL
     ELMRMNGSSQ KEMIEQAPSA YTSVFQKRVR LMAPLLKAWR AALKAEGAVD FSGLIHQAVN
     ILEKGRFISP WKHILVDEFQ DISPLRAKLL TALKMQNKQS HLFAAGDDWQ AIYRFSGAEL
     TLTTAFSDYF GKGAECTLDT TYRFSERIAE IANLFIQQNP SQLSKPLNSL VKGNKKSVVI
     LPEEQLETLL NKMSGYVTKQ ETILLLARYH YLKPKLLKKA STRWPNLNIE FMTIHASKGQ
     QADYVIILGL HHGQDGFPAP IRESVIEQAL LPKPEDFPDA EERRLLYVAL TRAKKQLWLM
     QEPKNPSIFI HQLGKLGVPT QRKP
//
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