ID B3EGK2_CHLL2 Unreviewed; 741 AA.
AC B3EGK2;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-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=Clim_0547 {ECO:0000313|EMBL:ACD89639.1};
OS Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290315 {ECO:0000313|EMBL:ACD89639.1, ECO:0000313|Proteomes:UP000008841};
RN [1] {ECO:0000313|EMBL:ACD89639.1, ECO:0000313|Proteomes:UP000008841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 245 / NBRC 103803 / 6330
RC {ECO:0000313|Proteomes:UP000008841};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Zhao F., Li T., Liu Z.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium limicola DSM 245.";
RL Submitted (MAY-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 -!- 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; CP001097; ACD89639.1; -; Genomic_DNA.
DR RefSeq; WP_012465520.1; NC_010803.1.
DR AlphaFoldDB; B3EGK2; -.
DR STRING; 290315.Clim_0547; -.
DR KEGG; cli:Clim_0547; -.
DR eggNOG; COG0210; Bacteria.
DR HOGENOM; CLU_004585_5_2_10; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000008841; 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 6..286
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 287..562
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 647..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 27..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 741 AA; 83837 MW; E779AEB97E87E8FF CRC64;
MTDFLRDLND VQRSAVTATE GPVMVLAGAG SGKTRVITYR IAHLIRNNGV TPYNILALTF
TNKAAGEMRH RIDKLLQSGS ASGLWIGTFH SVFARLLRSY IHLIGYDRNF SIFDSDDSKS
LIRQSMNELG ITHDSLPVNA VQSIISKAKN SFILPSEFQS RPGDYNQQKA AKVYELYTRK
LRENNALDFD DLLIKPLELF RAHEAVLGEL QETFRYILID EYQDTNRAQY LAAKMLGAKH
RNIFVVGDDA QSIYSWRGAD ITNILNFQDD YQDSQTFKLV ENYRSTGTIL QAANSVIRNN
HRQIKKDLIS NRSAGEPVTL IEAYNERQEG EKVVEHIRSM RQKDGHDYSG FAVFYRTNAQ
SRVLEDVMRQ NRIPYRIFGS VSFYKRKEIK DAVAYLRFIV NERDNESLLR IINFPPRKIG
DVSIAKLKEY AVLQDVSLYD AIRNAAEGGF QQRLVNALES FSSVIEQLRE LSEYGSVYDV
LSELYSLTAI PAQLQAENTA ESLARYDNLQ ELLSMARDFS DHNPDSSSLG DFLENISLAS
DYDETRESDN YVSLMTVHAS KGLEFPVVFI TGMEERLFPL STYEQDELEE ERRLFYVAMT
RAQEKIFLSW ARSRYQYGQP QQCLRSMFVT EIDASIVRTE SGELLSVRGS SERASSAGSS
PARGVQPRVP SPQNGIQAPR QESKPASKGF RAGAMVHHAL FGPGMILEVH GSGSGQKVKI
RFRTAGDKTL MVQYANLRIV S
//
