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Database: UniProt
Entry: Q8NPP6_CORGL
LinkDB: Q8NPP6_CORGL
Original site: Q8NPP6_CORGL 
ID   Q8NPP6_CORGL            Unreviewed;       785 AA.
AC   Q8NPP6;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 123.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   OrderedLocusNames=Cgl1765 {ECO:0000313|EMBL:BAB99158.1};
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=196627 {ECO:0000313|EMBL:BAB99158.1, ECO:0000313|Proteomes:UP000000582};
RN   [1] {ECO:0000313|Proteomes:UP000000582}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 /
RC   NCIMB 10025 {ECO:0000313|Proteomes:UP000000582};
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
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; BA000036; BAB99158.1; -; Genomic_DNA.
DR   RefSeq; NP_600969.2; NC_003450.3.
DR   AlphaFoldDB; Q8NPP6; -.
DR   STRING; 196627.cg1985; -.
DR   KEGG; cgl:Cgl1765; -.
DR   PATRIC; fig|196627.13.peg.1715; -.
DR   eggNOG; COG0210; Bacteria.
DR   HOGENOM; CLU_357058_0_0_11; -.
DR   OrthoDB; 3196263at2; -.
DR   BioCyc; CORYNE:G18NG-11357-MONOMER; -.
DR   Proteomes; UP000000582; 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   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; PF13245; AAA_19; 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}; Coiled coil {ECO:0000256|SAM:Coils};
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}; Reference proteome {ECO:0000313|Proteomes:UP000000582}.
FT   DOMAIN          10..262
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   COILED          574..613
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         31..38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   785 AA;  87595 MW;  AF0B1AE541320C94 CRC64;
     MAASGYQIQP HFSTQQREAI TTDNPLAIIQ AGAGTGKSTV ILERIEYLCA AGTNPEEIAV
     LSFTNAAADN ITAKNDKVTS MTISKMVHEI YAHNFPDHEI STIDTIINTL DIEYGDQMVT
     SDYMIQLRDL LYKVMTQGGN ANLTALSIFM ESHIEAFISV LDQIKQTSLE LEIIICYLLL
     DKLIEPHASP KYLIIDEVQD NSVFEFVFAL RFAAKHNTSL YLVGDSSQTL YEFRSANPKA
     LNSLEASGVF GTYRLTTNYR SNQEILDFAN IHLSDIEANQ FAGIQLYANS FDAPTADSFK
     EKVELDMHHV SKQSEFTDSI PYFMESNKAR FDAAILNNEQ TIVLAHSGRE IRAAQQALAE
     MYPSITVRNL QSDKGFNNTV FSTFIKDFWF EVTAVDPAHA AFTFTSQVTA HLDKLVRGKR
     EQMEDRVIRS MAAWWRENER DIQGWVQQTQ SGAITNEEFF YRLRQCILDY EIRNNRARQS
     MLNARNNANK EAVAQEKPLL MVSTIHSAKG LEFDNVIVLQ KPSSDAEMTE EGKRATYVAL
     TRAKKRELII AGSTRAYPRI VTDYEQIVDL LEKRDEERKI KEEEAAALAT LEAEQETRAL
     AAAEAQAQAL LLEHNPWLRD LSDEEVTALT EQEIINNVEA ALQIEEEEEE ARALAAAEPA
     IQQYLSQFAF DEFPDDDNVA NTVVHVAPQP ILHQAVPADV TVQSSTAPVT PVVADLEVTT
     VAADPVEPTI VAAQPEVDDN LVYSTSTPNS HSDVIAVNSD TSENAAVNPV LSDIEALRAI
     FNNQD
//
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