ID V4PE36_9CAUL Unreviewed; 756 AA.
AC V4PE36;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=AEAC466_12860 {ECO:0000313|EMBL:ESQ83560.1};
OS Asticcacaulis sp. AC466.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1282362 {ECO:0000313|EMBL:ESQ83560.1, ECO:0000313|Proteomes:UP000017826};
RN [1] {ECO:0000313|EMBL:ESQ83560.1, ECO:0000313|Proteomes:UP000017826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC466 {ECO:0000313|EMBL:ESQ83560.1,
RC ECO:0000313|Proteomes:UP000017826};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(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}.
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:ESQ83560.1}.
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DR EMBL; AWGE01000012; ESQ83560.1; -; Genomic_DNA.
DR AlphaFoldDB; V4PE36; -.
DR STRING; 1282362.AEAC466_12860; -.
DR PATRIC; fig|1282362.3.peg.2533; -.
DR eggNOG; COG0210; Bacteria.
DR OrthoDB; 9806690at2; -.
DR Proteomes; UP000017826; Unassembled WGS sequence.
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 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; 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; 2.
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:UP000017826}.
FT DOMAIN 10..291
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 292..563
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 673..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 31..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 756 AA; 85151 MW; 72DF5F852A781664 CRC64;
MAAVKSDFFA GLNAEQEAAV RTTQGPVLVL AGAGTGKTRV LTTRIAHILA QGLARPWEIL
CVTFTNKAAR EMRERTQKLV GASAEGLSHL GTFHSIAAQI LRRHAELVGL KSSFTILDDD
DQVRLLKAIF EQENIDQKRY TPKSFAWQID QWKNKGLTPD KVKGGDGAEF GGNKGIKLYQ
MYQDRLRILN ACDFGDLLLH NLEILTKHAD ILEHYHKRFK YVLVDEYQDT NIAQYLWLRI
LTNADRNLCC VGDDDQSIYG WRGAEVDNIL KFERDYPGAK IIRLERNYRS TQHILGAAAG
LIKANTARLG KTLFTDQVGG DKVQVQGLWD GAAEAQFVAE DMERLHKGTR DTSPRKWSDM
AILVRASFQM RAFEERFVML QIPYVVVGGP RFFERAEIRD AIAYLRLIQS PDDDLAFERI
INVPKRGIGD ATVQKLLQQA RLAGVSVMTA VRDLVQTDEL PSRTKTPLIG FLRDFQRWLD
LSKDTQADVL LDTVLTDTGY YDMQRADKTS GATRLDNLKE LGDSMQAFDN LEAFLEHVSL
VMDLERDNGG DSVRLMTLHA AKGLEFPVVY LPGWEEGIFP SQRSMDENGL RALEEERRLA
YVGITRARQE AKISFVANRQ VYGRWTNQIP SRFVDELPIE NVEATSQTGY AGQGWQSQQS
RWDRAGYEPN YTKKAASSDF GGNLSGIDMS RLAPKSTPHR PSPPPKPSAK NFKLGERVFH
MKFGYGEIVE IEGNKLVVNF ETSGDKKVID SFVDRA
//
