ID A0A3M8HDT3_9BACI Unreviewed; 1239 AA.
AC A0A3M8HDT3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 ECO:0000313|EMBL:RND00636.1};
GN ORFNames=EC501_04110 {ECO:0000313|EMBL:RND00636.1};
OS Lysinibacillus halotolerans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1368476 {ECO:0000313|EMBL:RND00636.1, ECO:0000313|Proteomes:UP000279909};
RN [1] {ECO:0000313|EMBL:RND00636.1, ECO:0000313|Proteomes:UP000279909}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1A12703 {ECO:0000313|EMBL:RND00636.1,
RC ECO:0000313|Proteomes:UP000279909};
RX PubMed=24814335; DOI=10.1099/ijs.0.061465-0;
RA Kong D., Wang Y., Zhao B., Li Y., Song J., Zhai Y., Zhang C., Wang H.,
RA Chen X., Zhao B., Ruan Z.;
RT "Lysinibacillus halotolerans sp. nov., isolated from saline-alkaline
RT soil.";
RL Int. J. Syst. Evol. Microbiol. 64:2593-2598(2014).
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}.
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:RND00636.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RHLQ01000006; RND00636.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M8HDT3; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000279909; Unassembled WGS sequence.
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 Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
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:UP000279909}.
FT DOMAIN 12..489
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 517..821
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1239 AA; 143655 MW; 48C48A7C4029F267 CRC64;
MGLSIPEKQP DVTWTDEQWK AIWATGQDTL VSAAAGSGKT AVLINRMIEK VISKENPIDV
DELLVVTFTN ASAAEMRHRM AEALEKEIAK DPRNQHLRRQ LSLVNKAQIS TLHSFCLAIV
RQYAYLIDID PGFRIANEGE SALLRDDVLA EVLEEAYDSE DEEKVNAVYR LVDSFTSDRD
DQAIETLIDK LYETSRVHPE PTKWLRSLPK QYDLPEHVTI DELDFIEPLK KSIKFSLEEA
REHIEEVRQL ALKPDGPYAY GETAELDFAL IEEAIRIMEH STWQVAYEFF NRLKWSTLAR
MKKDSCDPVL QERAKKKRDQ AKKILSQIKE SFFLRKPERL LQEIRLMAPI IKTLVELTEA
YSYKFKEAKL QRGLVDFSDL EHYALDILTV KEDGKLQPSP VALDFKQKFK EVLVDEYQDT
NMLQETILQL VKSGSEMDGN LFMVGDVKQS IYRFRLAEPM LFLNKYLHFE EEPVSNGLKI
DLNANFRSRQ EVLHGTNFVF EQIMGETVGE IIYDEKAGLK PGAPYDSVEM PIELAIIYEE
QEDDGEEIDE DAEMDFIIEE EIKKSQQEAR FIIKRIRELM DGGTTVYDTK QKDPAKRIRP
MKYSDIVILM RSMTWSNDLV EEFKAAGIPL FAESSKGYFE ALEVMVMLNV LKVVDNPYQD
IPLASVLRAP FIGCTENELA KIRLANRKAP FYEAVKQFVE EEQSGIHSET SEKLQRFLQQ
LDTWRNLARR GSLSDLIWRI YLDTNYYEMV GAMANGKQRQ ANLRTLHDRA LMYEKTSFRG
LFRFLRFIDR MRSRGDDLGV AKSIGEKDDV VRLVTIHSSK GLEYPVVFVA GLGRSFNQMD
FSNAYLFDQQ FGLAVKAIDP DDRIMYTSLP FLAMKEKKIL EMKAEEMRIL YVAMTRAKER
LILVGSVKDW EKVRSKWCEV QQLPTDLMLP EYLRARAKSY LDWIGPVVAR HASFEPFSDE
EYRPIDHPSK WRITPISNTF FMNSITSEQQ EEAGEQADTH LDEKVYNELR NRFTTGYPFK
NAILKKSKTS VSEIKRIENL QREEEETYPI QSTSSSAMKR PMFLQEKGLS ATEIGTVIHT
VMQHIPQRGF DRVEEVQAYL QSLVDRKLLT SEELAVVELE KVLQFFASDI GQRFSRAVQL
YREIPFTLSI EDEEGDSQIV QGILDCLFQD EQGRWVLLDY KTDKILPSFK EEPFLTNEMK
KRYEVQLRIY SEAIESILQV KVDEKVLYLY NAQKEIHFN
//
