ID F3KV87_9BURK Unreviewed; 1133 AA.
AC F3KV87;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
DE AltName: Full=DNA 3'-5' helicase II {ECO:0000256|ARBA:ARBA00034923};
GN ORFNames=HGR_11870 {ECO:0000313|EMBL:EGI76310.1};
OS Hylemonella gracilis ATCC 19624.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Hylemonella.
OX NCBI_TaxID=887062 {ECO:0000313|EMBL:EGI76310.1, ECO:0000313|Proteomes:UP000016368};
RN [1] {ECO:0000313|EMBL:EGI76310.1, ECO:0000313|Proteomes:UP000016368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19624 {ECO:0000313|EMBL:EGI76310.1,
RC ECO:0000313|Proteomes:UP000016368};
RX PubMed=21673657; DOI=10.1038/emboj.2011.186;
RA Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R.,
RA Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J.,
RA Jensen G.J.;
RT "Structural diversity of bacterial flagellar motors.";
RL EMBO J. 30:2972-2981(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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGI76310.1}.
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DR EMBL; AEGR01000073; EGI76310.1; -; Genomic_DNA.
DR RefSeq; WP_006298449.1; NZ_AEGR01000073.1.
DR AlphaFoldDB; F3KV87; -.
DR STRING; 887062.HGR_11870; -.
DR eggNOG; COG1074; Bacteria.
DR OrthoDB; 5905204at2; -.
DR Proteomes; UP000016368; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
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; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|PROSITE-ProRule:PRU00560,
KW ECO:0000313|EMBL:EGI76310.1};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000016368}.
FT DOMAIN 13..491
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 531..800
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1133 AA; 125120 MW; BAF17793A43931A6 CRC64;
MNMQAAYEHN GRHVSREAFY AIACDPRRHV AVEACAGAGK TWMLVSRILR ALLGEQGDDG
AQAHEILAIT FTKKAAGEMR QRLTEWLSAF ACYDDDQLRA ELRARGVEQA RVDVLIAPLR
GLHLRLLQQG RAVQIRTFHS WFAALLRNAP LAVLEELGLP AAYELLENDD EVKAQVWRPF
HARLLREQDQ GGTVLADYQA VVSRHGRSQT EKALEAVLDK RVEFALADAA GNVETSVPGF
AEVFPMFRGL ALPSQALLSE AVAARWRAWA QVLGQEKNKT PQTAAQAIEQ AFTQQADADQ
RLAALRKAVF VAEADRLTQH LKKYPAAQQA EAELQPLLQA QQQHEAWVHQ QRMIRLARIL
LEEYAALKRE RGWVDMSDVE RAALHLLERS ELSAWLQQRL DARTRHLLID EFQDTNPLQW
QALHAWLSSY AGVGGGASGA GGAPRLFIVG DPKQSIYRFR RAEPQIFRAA QSFVQALGGD
LLACDHTRRN APAVLARVNA VLGEAQSQGE YEGFRAHTTE STQAGQAWVL PPIERQARDK
KEAATVWRDS LLAPRLTPED TLRARECRQA ARWIAQRIEA GLPPKEVMVL ARKRDRLVAM
QAELLALGVP ATQPEQADLG AAPEVQDLTA LLDVLVSPGH DLSLARVLRS PLLGPHLGLD
DTALLEIAAR QRGGKQAWFD LLQTTPPAAW AHADLREVGP RLQRWQQWVR TLPPHDALDA
IYADGDVVAR YAAAAPPHLR ARVQTHLQAL LEAALQFDGG RYATPYALVR ALRAGRLPAP
AQPMPEGGAV RLLTVHGAKG LEAETVLILD TDTPPQRAQT MSVLLDWPGE ASAPRSFVFL
ASEKEERLPP SAREAHARER AARGREELNM LYVALTRARA QLVFSAVQPH QQNTEGKSWW
QRLLHECQPW EPTPPQSPAD GVARFEGMGR VSDMDGREAG APTQHEPAVA APAASSAIVL
RVLPDIRYQP VPVLAPSSEE DALAARIGSA MHRLLEWTAL DTAEFSPAQL ERAGAEQGLT
PAQARQAADM ARRIVHGAGA WVWRGADVAW WSNEVPVTIE GQARRIDRLV RHRDGTWWVL
DYKSASYAQA AEVTRAQMLA QLRAYGDAVR AACAGEPVRI ALLDAQGHWE TLA
//