ID D9SS52_CLOC7 Unreviewed; 648 AA.
AC D9SS52;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN OrderedLocusNames=Clocel_2802 {ECO:0000313|EMBL:ADL52499.1};
OS Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=573061 {ECO:0000313|EMBL:ADL52499.1, ECO:0000313|Proteomes:UP000002730};
RN [1] {ECO:0000313|EMBL:ADL52499.1, ECO:0000313|Proteomes:UP000002730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35296 / DSM 3052 / OCM 3 / 743B
RC {ECO:0000313|Proteomes:UP000002730};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA Hemme C.L., Woyke T.;
RT "Complete sequence of Clostridium cellulovorans 743B.";
RL Submitted (AUG-2010) 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 -!- SIMILARITY: Belongs to the peptidase S24 family.
CC {ECO:0000256|ARBA:ARBA00007484, ECO:0000256|RuleBase:RU003991}.
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DR EMBL; CP002160; ADL52499.1; -; Genomic_DNA.
DR RefSeq; WP_010076693.1; NC_014393.1.
DR AlphaFoldDB; D9SS52; -.
DR STRING; 573061.Clocel_2802; -.
DR KEGG; ccb:Clocel_2802; -.
DR eggNOG; COG0210; Bacteria.
DR eggNOG; COG1974; Bacteria.
DR HOGENOM; CLU_446699_0_0_9; -.
DR OrthoDB; 9787585at2; -.
DR Proteomes; UP000002730; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW.
DR CDD; cd06529; S24_LexA-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR039418; LexA-like.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006197; Peptidase_S24_LexA.
DR InterPro; IPR015927; Peptidase_S24_S26A/B/C.
DR PANTHER; PTHR33516; LEXA REPRESSOR; 1.
DR PANTHER; PTHR33516:SF13; PROPHAGE REPRESSOR COHE-RELATED; 1.
DR Pfam; PF00717; Peptidase_S24; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR PRINTS; PR00726; LEXASERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813,
KW ECO:0000256|RuleBase:RU003991}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003991};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000256|ARBA:ARBA00022825};
KW Reference proteome {ECO:0000313|Proteomes:UP000002730};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW SOS mutagenesis {ECO:0000256|ARBA:ARBA00023199};
KW SOS response {ECO:0000256|ARBA:ARBA00023236}.
FT DOMAIN 291..401
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13361"
FT DOMAIN 527..642
FT /note="Peptidase S24/S26A/S26B/S26C"
FT /evidence="ECO:0000259|Pfam:PF00717"
SQ SEQUENCE 648 AA; 74860 MW; 3EE2CEC453880937 CRC64;
MKRFVTSKPV KLTIIKGPSG TGKTTLAILR LSYLLNNYCQ EDKDSAILIT RNRLLRGYAR
YIYEGISGNG QLTLFSLLNI EKEILTLEGL KNLIIKKVFS SGYKVIKTKE EEIGFLKKAI
DEIKLKFKKS KLLKDYQYID FILEEINFIN SEGISSLEVY QNVKRYRNIP YPENIKKFVL
RKNSLGREVI YRINEAFNEI TKSQGYIKKE AKTNLAISLA IENNIKFTHI IIDDIDKFTR
SELELIKVLA SEKQHSTVTL TSRNRKAVLP YSYLGKGRTL KAIDLQGKTI LLKDSYRTNK
SICDFAESLM EKGKSRNTLL KSSLVSGIGE YPIHRNFSLE KEEYLYIARL IKEELTRKNK
YKDITILIKE HHYLERLKMF FYSNQIPYVF LDGKEFESNK EAVRISTYDI YSGLENRITI
ICGVNESSYN REEHRRFLYD QILSTKEKLY ITSSGKPSIF LDEVSPKLFK IDDRQYSDKG
LEHYTFLDFT RDKRIELIKD ITLSKNLSIK SEDSYVDVEE SELKRIPVFN NIAAGSPILI
NEEESDGFFL PKAFLKNNKE FFMLKVSGDS MINANLNNED YVIIERSAQV DNMQIAAVAI
GEEATLKRIK IKGNSVTLIS ENQNYPPMMV HSKDVRILGN AVGVIKKR
//
