ID F9VL32_ARTSS Unreviewed; 731 AA.
AC F9VL32;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN OrderedLocusNames=SFBM_1076 {ECO:0000313|EMBL:BAK56840.1};
OS Arthromitus sp. (strain SFB-mouse-Japan).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Candidatus Arthromitus.
OX NCBI_TaxID=1029718 {ECO:0000313|EMBL:BAK56840.1, ECO:0000313|Proteomes:UP000001636};
RN [1] {ECO:0000313|EMBL:BAK56840.1, ECO:0000313|Proteomes:UP000001636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SFB-mouse-Japan {ECO:0000313|Proteomes:UP000001636};
RX PubMed=21791478; DOI=10.1093/dnares/dsr022;
RA Kuwahara T., Ogura Y., Oshima K., Kurokawa K., Ooka T., Hirakawa H.,
RA Itoh T., Nakayama-Imaohji H., Ichimura M., Itoh K., Ishifune C.,
RA Maekawa Y., Yasutomo K., Hattori M., Hayashi T.;
RT "The lifestyle of the segmented filamentous bacterium: a non-culturable
RT gut-associated immunostimulating microbe inferred by whole-genome
RT sequencing.";
RL DNA Res. 18:291-303(2011).
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 -!- 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}.
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DR EMBL; AP012202; BAK56840.1; -; Genomic_DNA.
DR RefSeq; WP_005805686.1; NC_015913.1.
DR AlphaFoldDB; F9VL32; -.
DR STRING; 1029718.SFBM_1076; -.
DR KEGG; asf:SFBM_1076; -.
DR eggNOG; COG0210; Bacteria.
DR HOGENOM; CLU_004585_5_2_9; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000001636; 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; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
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};
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 5..284
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 285..559
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 26..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 731 AA; 84687 MW; 150883FF03D2FE37 CRC64;
MELRELLNEE QYSAVTTIDG PLLILAGAGS GKTRTITYRI AHMVKNLGIN SYQILAITFT
NKAAKEMKDR VRSLIGEISD NMWISTFHSL CVRILRREID KLGYTSSFTI YDFSDQKTLV
KQCMDILKIN QENIEPSEVL RRISNYKNQF IKPIEAISNT DNYREKLIAQ IYEIYEKKLF
ENNSLDFDNL IFKTIELFER FPEILSFYQS KFKYIMVDEY QDTNYAQYYL VKMLADMNKN
ICVVGDDDQC IYQWRGADIN NILDFEKDYK NTKIIKLEKN YRSKSNILDA ANKVILNNIK
RKKKILKATN NEGEKIKLFK ASSAEEEALF VINEIFRIIN SRGYEYRDFG ILYRTNSQSR
MFEEICVKNQ IPYKLVGVMR FYERKEIKDV IAYIKTIVNP SDEISLRRII NEPKRGIGDT
TLSKLLEYAE RNGISLFDSM VACADIETIS LRTQDIIKNF AKSIEEIRKY IDLNPSEFIR
LMLDKIGYID ALKKSKDSDI DTRFENIQEF INASVNFEQL NIGSNIEDFL ENISLVSETD
KYDEKSSSIT LMTIHSSKGL EFPVVFMVGM ENGIFPSNKC FDEIDEMEES RRLCYVGITR
AKDILYFTYA NMRMVYGETG FRTKSKFLGE VPSDLMLNIN FKGEEITLSQ SMPSRSFGKF
SYNPLDNDIS KKCNDVSKDD VKIGMKIKHK NFGLGMVVKV EDDPESPKVI VAFDNNGIKK
LALNNAPIEF V
//
