ID E3EKZ6_PAEPS Unreviewed; 737 AA.
AC E3EKZ6;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=PPSC2_28660 {ECO:0000313|EMBL:ADO59901.1};
OS Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OG Plasmid pSC2 {ECO:0000313|EMBL:ADO59901.1,
OG ECO:0000313|Proteomes:UP000006868}.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO59901.1, ECO:0000313|Proteomes:UP000006868};
RN [1] {ECO:0000313|EMBL:ADO59901.1, ECO:0000313|Proteomes:UP000006868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2 {ECO:0000313|EMBL:ADO59901.1,
RC ECO:0000313|Proteomes:UP000006868};
RC PLASMID=pSC2 {ECO:0000313|Proteomes:UP000006868};
RX PubMed=21037012; DOI=10.1128/JB.01234-10;
RA Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.;
RT "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant
RT growth-promoting Rhizobacterium with broad-spectrum antimicrobial
RT activity.";
RL J. Bacteriol. 193:311-312(2011).
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; CP002214; ADO59901.1; -; Genomic_DNA.
DR RefSeq; WP_013386315.1; NC_014628.2.
DR AlphaFoldDB; E3EKZ6; -.
DR KEGG; ppm:PPSC2_28660; -.
DR PATRIC; fig|886882.15.peg.6082; -.
DR eggNOG; COG0210; Bacteria.
DR HOGENOM; CLU_004585_6_1_9; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000006868; Plasmid pSC2.
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 GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR CDD; cd17932; DEXQc_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; 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}; Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Plasmid {ECO:0000313|EMBL:ADO59901.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006868}.
FT DOMAIN 15..310
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 311..572
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 737 AA; 85181 MW; F7D30043EE096F43 CRC64;
MEVDFFEQKK QETGVNLSAV QREAVEHTEG ALLVLASPGS GKTTMMIMKI GYLIEEKDVD
PSRIRAVTFS NASATDMDNR FDKLFPHLKD NKVKFSTIHS FAFEVVRAYF KKNNIRYQLI
EGNMDKPNSE PCRVVNKLNK RIILRRIFRE VTQENVTEEQ MEELLSYISY IKNKLIPYDQ
LEDIETSIPS ASEIFLSYEE FKCADFTNRL VDYDDMLVIA NDALEKDAGM LAEYQSMFDY
FLTDESQDNS LVQNLIIEKL VRLKGNICVV ADDDQSIYGW RGAAPEYLLN FKEVYPNAKI
LYMVQNYRST KDIVEVANQF IKRNKNRYDK EMFTEKESFK PIQLSHLDTY EAQIRHIVEK
VKYAPVKKEV AILYRNNSSS IALIDELEHQ GIPFYIKDSD NKFFSHWIIE DILNFMRMSY
SDKHPILLEK IHTKFNGYIN KPQIEYLKEI NNKASVFDNL LKLNVPVYQR KNLGKCKEIF
KRINQLRPDQ AIRVIRDELG YEKKLVKMCE SLGFKKEYLL SILNTLQGIG SKLETLKDFA
ERLNYLRKVL SQSKFEKGKD VVTLSTFHSS KGLEFNQVIM IDLIEGVIPS KEVIKDFKSG
KIDEMEEAVR LFYVGMTRAR TDLELISYKR KDGESVQESS FVKDVKQIMF PNKGSKKKNV
NQAKKIAFSD RSNAFKNIEE VTIGSKVKHA TFGLGNIINV DTQIISIRFE KIGMKNLAAK
ICIEKGLLEA VAIADVG
//
