ID K7RTE7_ACIA4 Unreviewed; 557 AA.
AC K7RTE7;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=UvrD/REP helicase {ECO:0000313|EMBL:AFV88178.1};
DE EC=3.6.1.- {ECO:0000313|EMBL:AFV88178.1};
GN OrderedLocusNames=PACID_03290 {ECO:0000313|EMBL:AFV88178.1};
OS Acidipropionibacterium acidipropionici (strain ATCC 4875 / DSM 20272 / JCM
OS 6432 / NBRC 12425 / NCIMB 8070 / 4) (Propionibacterium acidipropionici).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Acidipropionibacterium.
OX NCBI_TaxID=1171373 {ECO:0000313|EMBL:AFV88178.1, ECO:0000313|Proteomes:UP000000214};
RN [1] {ECO:0000313|EMBL:AFV88178.1, ECO:0000313|Proteomes:UP000000214}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 4875 / DSM 20272 / JCM 6432 / NBRC 12425 / NCIMB 8070
RC {ECO:0000313|Proteomes:UP000000214};
RX PubMed=23083487; DOI=10.1186/1471-2164-13-562;
RA Parizzi L.P., Grassi M.C., Llerena L.A., Carazzolle M.F., Queiroz V.L.,
RA Lunardi I., Zeidler A.F., Teixeira P.J., Mieczkowski P., Rincones J.,
RA Pereira G.A.;
RT "The genome sequence of Propionibacterium acidipropionici provides insights
RT into its biotechnological and industrial potential.";
RL BMC Genomics 13:562-562(2012).
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};
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DR EMBL; CP003493; AFV88178.1; -; Genomic_DNA.
DR RefSeq; WP_015069095.1; NC_019395.1.
DR AlphaFoldDB; K7RTE7; -.
DR STRING; 1171373.PACID_03290; -.
DR KEGG; pbo:PACID_03290; -.
DR PATRIC; fig|1171373.8.peg.328; -.
DR eggNOG; COG0210; Bacteria.
DR HOGENOM; CLU_004585_6_1_11; -.
DR Proteomes; UP000000214; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
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; 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; PF00580; UvrD-helicase; 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};
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 2..270
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT BINDING 23..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 557 AA; 61669 MW; 2E9B7C6F35F295F0 CRC64;
MVTPTAAQVQ IRDHEGLSLR VAAPAGCGKT EALALRVAGL ISRGVASGPR RILVMTFSNR
ARDNIRDRLQ SYVPLSVLRD SVSLTNFHGL SARIFRAHGR VIGLDPEMVL PESDWVREQC
FRWRWGWDKI KPSENALRLA KQQALDDAEV ERFLRAHDSN GALQLERQRL AEKRLTYDDL
PRVAELLLND DAVASLYRNH FSAVIVDEFQ DLTPQQLRIV NRIGLGKTTY AGDLAQGIYS
FAGAQPARVE RAIRLECADA IELSESHRSS PAVLSMVNSL RELTGGAKLT SACPESWPGG
GLAAGVVFKD PEEEGRWAVE FSRYILARAP RQRIAIICRN GPRRKAVDTL AKMSGLPVYI
WDDGMLDTET ARLVKGMLGR LDSDKAVAAA DPLQYLRDAI NFDAIVDIDT RRPLYDALVW
CLGKLRDGNT PIQIRNRIGV GGQETLLTAA GLHLLSGHVG KGQQFDWVVA VGVEDGVIPD
WRSNEEAEKM EDARVLSVML SRARIGVVVT FATQVADNSG RLRSRKGSPF LQQLKTALPT
DEAGVHRFLE SRDWDSM
//
