ID A0A3N9UIY4_9BACI Unreviewed; 1243 AA.
AC A0A3N9UIY4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
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:RQW75398.1};
GN ORFNames=EBB45_06530 {ECO:0000313|EMBL:RQW75398.1};
OS Lysinibacillus composti.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=720633 {ECO:0000313|EMBL:RQW75398.1, ECO:0000313|Proteomes:UP000274033};
RN [1] {ECO:0000313|EMBL:RQW75398.1, ECO:0000313|Proteomes:UP000274033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1A12701 {ECO:0000313|EMBL:RQW75398.1,
RC ECO:0000313|Proteomes:UP000274033};
RX PubMed=23812821; DOI=10.1007/s12275-013-2664-1;
RA Kim S.J., Jang Y.H., Hamada M., Ahn J.H., Weon H.Y., Suzuki K., Whang K.S.,
RA Kwon S.W.;
RT "Lysinibacillus chungkukjangi sp. nov., isolated from Chungkukjang, Korean
RT fermented soybean food.";
RL J. Microbiol. 51:400-404(2013).
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:RQW75398.1}.
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DR EMBL; RRCT01000004; RQW75398.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N9UIY4; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000274033; 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 CDD; cd17932; DEXQc_UvrD; 1.
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:UP000274033}.
FT DOMAIN 12..489
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 526..824
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 1243 AA; 143387 MW; FC25834DF5AE1293 CRC64;
MALSIPTKGP DVTWTDEQWK AIWATGQDTL VSAAAGSGKT AVLINRMIEK VISEDNPIDV
DELLVVTFTN ASAAEMRHRM AEALEKEIAK NPQNQHLRRQ LSLVNKAQIS TLHSFCLSIV
KQYAYLIDID PGFRIANEGE SALLRDDVLA EVLEAAYDQE DEEKVNAVYR LVDSFTSDRD
DQAIEILIDK LYEMSRVHPE PTKWLRSLPE QYDLPENITV DDLPFIEPLK KAIKFSLEEA
LAHIQEVRQY ALKPDGPAPY AETAELDFGL IQEAIRRIDN CSWQEIYDYF VTLKWARLAS
VKKDSCDPDL QEKAKKKREQ AKKVMTTIKD SFFARKPERL LVEIRLMAPM ISTLVELTER
FGERFTTAKL ERGLVDFSDL EHFALQILTE EADGILVPSQ VAKDFQQRFK EVLVDEYQDT
NNLQETILQL VKSGNEANGN MFMVGDVKQS IYRFRLAEPM LFLNKYNQFE EEPEQNGLRI
DLNANFRSRQ EVLQGTNFVF EQIMGETVGE IDYDEKAGLK PGAPYNEAEM PIELTILHEE
QEDDHEQDET DEEIEAMDLV IEEEIKKSQQ EARYIIMRIR ELIDSGATVY NAKEKERAKR
ERPMRYSDIV ILMRSMTWSS DLVEEFKAAG IPLYAESSKG YFEALEVMVM LNVLKIVDNP
YQDIPLASVL RAPFVGLTEN ELAQVRLTNK KAAFYDALKE FVMEEKSGLT HQTAQKLQTF
LQQLETWRNL ARRGSLSDLI WKIYIDTNYY EMVGAMANGK QRQANLRTLH DRALMYEKTS
FRGLFRFLRF IDRMRSRGDD LGVAKAIGEK DNVVRLETIH SSKGLEYPVV FVAGLGRSFN
QMDFNNPYLF DQQFGLAVKA IDPDNRIMYT SLPFLAMKEK KILEMKAEEM RVLYVAMTRA
KERLILVGSV KNWDKVRQAW CEMQSLPHES LLPEYLRARA KTYLDWIGPA VARHKCFNEF
SEEDYRPIEH LSKWKITVLS NETFKFGSEN ETLASELNVM EQQVDEQLLN ELTKRFTTKY
PFSNSITKKS KTSVSEIKRI ESLQRDEEQE TAVFNRQKSS ATKRPQFLQE KSLSATEIGT
VVHTVMQHAP KEGFANVREV EAYLEALVER QLLTSDEIKV VELEKVFNFF ATSIGKRFSS
AKQLLREVPF TLSISDEEGD SQIIQGIIDC LFEDEDGKWV LLDYKTDKVL PGFKEEPALT
KEMTKRYGVQ LRIYSEAIED ILQIKVDEKI LYLYHVEKEI QLV
//
