ID   B4SNF4_STRM5            Unreviewed;       917 AA.
AC   B4SNF4;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   OrderedLocusNames=Smal_2478 {ECO:0000313|EMBL:ACF52179.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF52179.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF52179.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF52179.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Taghavi S.,
RA   Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) 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};
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DR   EMBL; CP001111; ACF52179.1; -; Genomic_DNA.
DR   RefSeq; WP_012511460.1; NC_011071.1.
DR   AlphaFoldDB; B4SNF4; -.
DR   STRING; 391008.Smal_2478; -.
DR   KEGG; smt:Smal_2478; -.
DR   eggNOG; COG0210; Bacteria.
DR   eggNOG; COG0551; Bacteria.
DR   HOGENOM; CLU_006494_1_0_6; -.
DR   OrthoDB; 5298826at2; -.
DR   Proteomes; UP000001867; Chromosome.
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; cd18807; SF1_C_UvrD; 1.
DR   Gene3D; 3.30.65.10; Bacterial Topoisomerase I, domain 1; 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}.
FT   DOMAIN          211..676
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   BINDING         232..239
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   917 AA;  103691 MW;  484EEB74DB317EAE CRC64;
     MEWRPSGWGL RVTRSPGWQL WLDGEHIELL IEGRQYRQHV ADDERVQVIP GLFWAKVILQ
     TQGDGVLTMN GLPNGQASRL AAALQQVRFA GTTRGRKALF DTILEQIQSW LAEADALIDR
     GSTGRRWITH EQQQALLAGR PGLPLPQREL EQLFLDEDVH EDLHSPSHRV ALDALHDWQL
     DWPTAWADAN ATMAARERVL AKDFLDRVES KPLTDEQARA VICFDNRVQV VASAGSGKTS
     TMVAKAAYAI DRGFVEPERI VMLAFNKDAA RELEERAQRC FDRLGMGDTV VEARTFHALG
     LAIVAKATGR KPDIAEWTTD ATLGFNKLAE LVDDLKDRST HFRTQWDMFR LVFGRDLPPF
     GTEMEADGYD RDGTPYIRTL QGERVKSLEE CVIADWLFYN GVTYDYERRY EFDTATDTHR
     QYRPDFYYPD AQLYHEHFAL DADGQPPKHF ANYSEGMHWK RQQHVARGTA LVETTSFGLR
     SGHALLDLAE KLGECDIELD PNPDRELPDQ GAKPMPDADL IGLMRTFIAH AKSNCLTLDD
     MAARLRQMPE DQFKERHRRF LEIAGPVFQA WDNALADERG IDFEDMLNMA AGLLEQGRYE
     SPYDLVMADE FQDASRARAR LCRALVSQPG RHLFAVGDDW QSINRFAGAD VSVMTGFREW
     MGHGQVLKLE QTFRCPQALC DVSGRFISRN PAQITKEVRS AAPAMGPVLQ AFQMNRREEV
     QDGVRQYLAK LHQQLLSGAV PQGRNGRVTV FILGRYRADR SAMPSDWKTA FGSTMEVEFL
     TAHRSKGREA DYVILPGMIN RSFPSLRADD PALSLAMPDG DTYPLSEERR LFYVALTRAR
     RSVSMFTLQG KRSPFLDELV KDGAVKVTAI SGAAINEERC PVCKVGVFVD RNGPHGTFRS
     CSSYPLCHNK PKGERRR
//