ID A0A097QXQ0_HAFAL Unreviewed; 720 AA.
AC A0A097QXQ0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
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 Name=uvrD {ECO:0000313|EMBL:AIU71254.1};
GN ORFNames=AT03_01835 {ECO:0000313|EMBL:AIU71254.1};
OS Hafnia alvei FB1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Hafnia.
OX NCBI_TaxID=1453496 {ECO:0000313|EMBL:AIU71254.1, ECO:0000313|Proteomes:UP000029986};
RN [1] {ECO:0000313|EMBL:AIU71254.1, ECO:0000313|Proteomes:UP000029986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB1 {ECO:0000313|EMBL:AIU71254.1,
RC ECO:0000313|Proteomes:UP000029986};
RX PubMed=25075225; DOI=10.1186/1757-4749-6-29;
RA Tan J.Y., Yin W.F., Chan K.G.;
RT "Gene clusters of Hafnia alvei strain FB1 important in survival and
RT pathogenesis: a draft genome perspective.";
RL Gut Pathog. 6:29-29(2014).
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; CP009706; AIU71254.1; -; Genomic_DNA.
DR RefSeq; WP_025802146.1; NZ_CP009706.1.
DR AlphaFoldDB; A0A097QXQ0; -.
DR GeneID; 78450939; -.
DR KEGG; hav:AT03_01835; -.
DR PATRIC; fig|1453496.5.peg.366; -.
DR eggNOG; COG0210; Bacteria.
DR HOGENOM; CLU_004585_5_5_6; -.
DR OrthoDB; 9806690at2; -.
DR Proteomes; UP000029986; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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:0006268; P:DNA unwinding involved in DNA replication; IEA:InterPro.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR CDD; cd18807; SF1_C_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; IPR005753; DNA_helicase_ATP-dep_UvrD.
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 NCBIfam; TIGR01075; uvrD; 1.
DR PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF21196; PcrA_UvrD_tudor; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000029986}.
FT DOMAIN 8..286
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 287..564
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 29..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 720 AA; 81783 MW; 2552CC0FE1ABAF67 CRC64;
MDVSDLLNSL NDKQREAVAA PRSNLLVLAG AGSGKTRVLV HRIAWLLSVE NCSPFSIMAV
TFTNKAAAEM RHRIEHLIGT SQGGMWIGTF HGLAHRLLRA HHLDANLPQD FQILDSDDQL
RLLKRIVKAL NLDEKQWPPR QGMWYINNKK DDGLRPQHIE SYGNPVEQTW LRVYQAYQEA
CDRAGLVDFA ELLLRAHELW LNKPQILNHY RERFTNILVD EFQDTNRIQY AWIQMLAGNS
GKVMIVGDDD QSIYGWRGAQ VENIQRFLDD FPGAETIRLE QNYRSTSNIL KAANALIENN
DGRLGKKLWT EDGDGEKISL YCAFNELDES RFVVNRIKAW QDNGGSLNDC AILYRSNAQS
RVLEEALLQV AMPYRIYGGQ RFFERQEIKD ALAYLRLISN RNDDAAYERV VNTPTRGIGD
RTLDVIRQAA RDRQLTLWQA THELIQEKVF AGRASGALQR FIELIDALAS DTADMPLHVQ
TDRVVRDSGL RQMYEQEKGE KGQTRIENLE ELVTATRQYS YEDEDEDLLP LQAFLSHAAL
EAGEGQADAY QDAVQLMTLH SAKGLEFPQV FIVGMEEGMF PSQMSLDEGG RLEEERRLAY
VGVTRAMRKL TITYAETRRL YGKEVYHRPS RFIGELPEEC VEEVRLRASV TRPVKHASMG
TPISANDSGF KLGQRVKHAT FGEGTVINLE GSGEHSRLQI AFQGEGIKWL VAAYAKLEAM
//
