ID A0A377KM64_9ENTE Unreviewed; 1239 AA.
AC A0A377KM64;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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:STP30063.1};
GN ORFNames=NCTC8129_02299 {ECO:0000313|EMBL:STP30063.1};
OS Enterococcus durans.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=53345 {ECO:0000313|EMBL:STP30063.1, ECO:0000313|Proteomes:UP000254070};
RN [1] {ECO:0000313|EMBL:STP30063.1, ECO:0000313|Proteomes:UP000254070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC8129 {ECO:0000313|EMBL:STP30063.1,
RC ECO:0000313|Proteomes:UP000254070};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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; UGIF01000002; STP30063.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A377KM64; -.
DR Proteomes; UP000254070; 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; 1.10.274.50; -; 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; 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; 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}; Coiled coil {ECO:0000256|SAM:Coils};
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}.
FT DOMAIN 11..480
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 507..798
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT COILED 62..89
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1239 AA; 144262 MW; EB743525F2682112 CRC64;
MNQIPLKPEN ERFTDEQWQA IFDQGDNLLV SASAGSGKTT VLVRRVIEKL KMGVNLDELL
IVTFTEAAAR EMKERIQEAL QEAVNTESDP IRQQHFTKQL VLLPTANIST LHAFCLTVIR
RYYYLIDIDP VFRMLTDETE TILMKEDVWD ELREAFYAEN REEFFRLTMN FSNDRSDDGL
TNLVFSLYEF ARANPDPEEW LTKLSESYRL ENELADSDLY KTQLRPLILA DMHQCVQLYE
EMVQLAQEEG LEKMYNQVSG EKGQIQVIYE HLLQDQIPEA YSGLEALTFT TFKSSRKAEL
KERSAEVKEL RDRAKKIIQQ LGKNYFPVSP EQMEELTKKA YPLVKEMTKV TKAFMNGFSQ
RKREKGLLDF NDLEHFALQI LTKKTDDTWL PSVASDHYRK QFKEVMVDEY QDVNQLQEAI
LYWLREPNET NGNMFMVGDV KQSIYSFRLA DPSLFIQKYE AFSKTEGGRR IVLAENFRSR
KEVLSFTNLV FEQIMDPVVG QISYDDAAKL VLGFPNFPET EQFEPEILIY EKEQEETTIE
LPVDDILEDK TEGELFMTGL KIRQLVDEKF MIYDKKMKKN RPIEYRDIVL LTPTKKNNLT
FLEIFKTFDI PLEMNDAQNY FQATEIRTMV SLLQLIDNPY QDIPLASVLR SPIVGLIEPE
LARIRLADRS HTYYEAVLAY QAEHTDELAD KLNHFGEQLE IWRELARRSS ITDLLWSIYY
QTGYLEYVAG LPAGAQRQAN LYALVDRAKS YEKSSFRGLY QFVRFIEKMQ EKDKDLAEPV
LASVDNAVRV MTIHASKGLE FPVVFLLDMT KQFNLQDLRK RYAFEEKLGA GIRYMDPDTR
VLYDTLPYQA IKLAKQNKLL SEEMRKLYVG LTRAEQKLFI VGSYKNKEET LKIWSEVANQ
TSLVLEPSTR LKGKGSLLNW IGYSLMRHPK MKEYAEDTTV HNQLGQSESR FSITWMKQQD
IVENRQSLAS ETKKELESVE VDQTPLQESL KARLAYSYPY KASTQTTSYQ SVSEIKRLFE
DPDDTSDSKL VWENNEKRRY NQQFRYTQDT LAEPKFLQKS QKISAASIGT ATHYLLQLLP
LEMPTNDSIR SLLEELVAKR LVDEKVAKKI DLSGILWFYQ TELGKRLVQH SELVKREQPF
SMLLSANQVF DQYPNEDDEL LIHGIVDGYI EFPEFIELYD FKTDYISNGE NQAEIETIVQ
KYQGQLNLYK KALSEALDKP VTNVYLILLG AKKIINLNK
//
