ID B2TIZ6_CLOBB Unreviewed; 750 AA.
AC B2TIZ6; U4P4Y1;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364053};
DE EC=5.6.2.4 {ECO:0000256|RuleBase:RU364053};
GN OrderedLocusNames=CLL_A0408 {ECO:0000313|EMBL:ACD25019.1};
OS Clostridium botulinum (strain Eklund 17B / Type B).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=935198 {ECO:0000313|EMBL:ACD25019.1, ECO:0000313|Proteomes:UP000001195};
RN [1] {ECO:0000313|Proteomes:UP000001195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eklund 17B / Type B {ECO:0000313|Proteomes:UP000001195};
RA Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Complete sequence of Clostridium botulinum strain Eklund.";
RL Submitted (APR-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,
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}.
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DR EMBL; CP001056; ACD25019.1; -; Genomic_DNA.
DR AlphaFoldDB; B2TIZ6; -.
DR KEGG; cbk:CLL_A0408; -.
DR PATRIC; fig|935198.13.peg.384; -.
DR HOGENOM; CLU_004585_5_2_9; -.
DR Proteomes; UP000001195; Chromosome.
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; IPR018247; EF_Hand_1_Ca_BS.
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; PS00018; EF_HAND_1; 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}.
FT DOMAIN 5..285
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 286..561
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 644..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 26..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 750 AA; 85646 MW; A19669F640F542CD CRC64;
MELKSLLNKE QYEGAITIDG QLLILAGAGS GKTRVLTYRM AHMIENIGIA PYNILAITFT
NKAAKEMKDR VISLIGSKAE NMWISTFHST CVRILRREID KIGYNSNFTI YDTSDQKVLI
KECMKLLNIN DKDISDQEIL SKIGKAKDTM QTAQSFMIQN ESNFREKKIA EAYEMYQRRL
KENNALDFDD LIFKAVELFK SNPEVLDFYQ NKFKYIMVDE YQDTNGAQYE LIKLLASKYK
NICVVGDDDQ CIYQWRGADI QNILDFEKDY PKAKVIKLEQ NYRSKSNILN AANVVIVNNA
NRKSKVLRTE QEAGDKIKIY RAFSDSDEGD FVSKQIAEIK SKENKEYKDF AILYRTNAQS
RIFEESLRRR GIPYKIIGGT RFYDRKEIKD VLAYLKAIVN PRDDVSLKRI INVPKRSIGD
ATVSKIQEFA NNFELDMWDA LMEVRTIPTL TPRNANNIEA FTNLMEEFMS LSETAPISVL
IEAILKETEY LKQLEASKEI EDKSRIENLK ELVSDAVDFE KNNEDKSLAA YLEKVSLVQD
TDKIEEQEDT IVLMTVHSAK GLEFPVVFMV GMENGIFPGN MSFEKESEME ESRRLCYVGI
TRAKETLFMT SAEVRRVFGR TVAYSQSDFI NEIKQELKEY VSGNRIGSGN GSNSNVKAQK
NDSYSNPHSL RSTIRKEFSK PVNTVINDND NSGYLNANEV TLGRKVQHEK FGIGTIVSVQ
GSGDDKKLTI AFDKQGVKNL MLSFAKLKAI
//
