ID A0A0U2KX10_9BACL Unreviewed; 1322 AA.
AC A0A0U2KX10;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=ATP-dependent helicase/nuclease subunit A {ECO:0000256|HAMAP-Rule:MF_01451};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01451};
DE EC=5.6.2.4 {ECO:0000256|HAMAP-Rule:MF_01451};
DE AltName: Full=ATP-dependent helicase/nuclease AddA {ECO:0000256|HAMAP-Rule:MF_01451};
DE AltName: Full=DNA 3'-5' helicase AddA {ECO:0000256|HAMAP-Rule:MF_01451};
GN Name=addA {ECO:0000256|HAMAP-Rule:MF_01451};
GN ORFNames=IJ22_09160 {ECO:0000313|EMBL:ALS21298.1};
OS Paenibacillus naphthalenovorans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=162209 {ECO:0000313|EMBL:ALS21298.1, ECO:0000313|Proteomes:UP000061660};
RN [1] {ECO:0000313|Proteomes:UP000061660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32O-Y {ECO:0000313|Proteomes:UP000061660};
RA Butler R.III., Wang J., Stark B.C., Pombert J.-F.;
RT "Complete genome sequences of two moderately thermophilic Paenibacillus
RT species.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALS21298.1, ECO:0000313|Proteomes:UP000061660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32O-Y {ECO:0000313|EMBL:ALS21298.1,
RC ECO:0000313|Proteomes:UP000061660};
RX PubMed=26868401;
RA Butler R.R.III., Wang J., Stark B.C., Pombert J.F.;
RT "Complete Genome Sequences of Two Interactive Moderate Thermophiles,
RT Paenibacillus napthalenovorans 32O-Y and Paenibacillus sp. 32O-W.";
RL Genome Announc. 4:e01717-15(2016).
CC -!- FUNCTION: The heterodimer acts as both an ATP-dependent DNA helicase
CC and an ATP-dependent, dual-direction single-stranded exonuclease.
CC Recognizes the chi site generating a DNA molecule suitable for the
CC initiation of homologous recombination. The AddA nuclease domain is
CC required for chi fragment generation; this subunit has the helicase and
CC 3' -> 5' nuclease activities. {ECO:0000256|HAMAP-Rule:MF_01451}.
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, ECO:0000256|HAMAP-
CC Rule:MF_01451};
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|HAMAP-Rule:MF_01451};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01451};
CC -!- SUBUNIT: Heterodimer of AddA and AddB/RexB. {ECO:0000256|HAMAP-
CC Rule:MF_01451}.
CC -!- SIMILARITY: Belongs to the helicase family. AddA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01451}.
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DR EMBL; CP013652; ALS21298.1; -; Genomic_DNA.
DR RefSeq; WP_062407541.1; NZ_CP013652.1.
DR STRING; 162209.IJ22_09160; -.
DR KEGG; pnp:IJ22_09160; -.
DR PATRIC; fig|162209.4.peg.977; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000061660; Chromosome.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 6.10.250.2380; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR HAMAP; MF_01451; AddA; 1.
DR InterPro; IPR014152; AddA.
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 NCBIfam; TIGR02785; addA_Gpos; 1.
DR PANTHER; PTHR11070:SF48; ATP-DEPENDENT HELICASE_NUCLEASE SUBUNIT A; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01451};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01451};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01451};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01451};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01451}; Reference proteome {ECO:0000313|Proteomes:UP000061660}.
FT DOMAIN 11..484
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 525..863
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 545..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1322 AA; 150206 MW; 63ED7D0985D9985B CRC64;
MTVTIPKPAG STWTDEQWNA ISVHGQSILV AAAAGSGKTA VLVERIIRRI SDERNPTDVD
RLLVATFTKA AAEEMRHRIS EALEKALAAN PESDHLRRQL ALIPRASITT LHSFCMEVIQ
KHYQVIGLDP GFRIANETES ALLRQDVLEE LLEERYGDSA EDDPFWRLAD AFSSDKSDDA
LFQLVQRIYD DARSHPWPEH WLEESVGRFE RCSMAGENPW QSSLQAYIRL ELQGIDALLR
EAVRTAEAPF GPEPYLANLN EDLTVIQSLL EAAADPSWHR LYQAFQGAGF GKLKACKGEQ
YDKELQEQVK ALRNEAKERL GDLKEELFVR TPEQYEEELR MMAPLMRTLA DLVIEFGERY
RKVKLDKGLV DFADLEHYCL RILSSDRSAP GAPVPSQAAL EYREQFVEVL LDEYQDTNRV
QEAIVELISR ESPGNRFMVG DVKQSIYRFR LAEPSLFQEK YKSFTPDGAD PGRRIDLARN
FRSRRQVVDG TNYIFRQLMN ENVGEIAYDQ KAELVYGAGY PETGNGNFDL ASKLILIDRS
AHDESVSGKK TEDESVTDSD QDPEADGASE DPAENRQELE TAQLEARYIA QQIRLMMGMD
GGEPFRVFDK SLKGLRPAAF RDFVILLRAT QQWAPVLIEE LRQQGIPAYA ELNTGYFTAT
EIQVVLSLLK LIDNPYQDIP LASVLRSPIV GMDSEELAHI RICSRHGAFF DAVRAYARKD
ETETEEAGEL SDPDGSEPSG DGDGAYIPKP ETQRKARSFL EQLNDWRRMA QQGSLADLIW
DIYRKTGYFD FVGGLPGGQQ RQANLRALYD RSRQYEATSF RGLFRFLRFV ERMQNSGGDL
GTARALGEQE DVVRIMTIHK SKGLEFPVVF AAGMAKPFNR RDLTDSFLLH KELGFGPKLT
DPKTRVSYPT LPWLAIKRKI QMEMLAEEMR VLYVALTRAR EKLVLVASVK GLEKQLKAWS
RFVLHDRLAL PDDALAKAKC YLDWIGPAMI RHPDGKLLRE GAGVEDTVPL FLKDESSEWR
VHLIMPELFA GMAQAAAGSD HADSRWQSVV RMEPVDETER WEHEVWRRLS WDYSYKDATL
VLSKTSVTEL KRLSEHHKLL ELLSEEPAAA PWHAAENGQD NVDKKGRDKG QTVFRRMIVR
RPRFMEQREL NAAERGSVFH SVMQHMPLDR HPSEADVRET LAWMVSRELL TEQQQSLVDP
AVIVSFFRSE LGQRLLQAKR VHREVPFSFG LPATDVYGAE PGGLSQETVM LQGVIDCLID
EEEGLVLLDY KTDRLKGASP QRVAESYRMQ LDLYARAVET IWKRPVIGKY IFLFDGAHVV
QL
//
