ID A0A0R2NJY1_9LACO Unreviewed; 1236 AA.
AC A0A0R2NJY1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=IV88_GL000969 {ECO:0000313|EMBL:KRO26055.1};
OS Pediococcus argentinicus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Pediococcus.
OX NCBI_TaxID=480391 {ECO:0000313|EMBL:KRO26055.1, ECO:0000313|Proteomes:UP000051249};
RN [1] {ECO:0000313|EMBL:KRO26055.1, ECO:0000313|Proteomes:UP000051249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23026 {ECO:0000313|EMBL:KRO26055.1,
RC ECO:0000313|Proteomes:UP000051249};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRO26055.1}.
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DR EMBL; JQCQ01000003; KRO26055.1; -; Genomic_DNA.
DR RefSeq; WP_057797949.1; NZ_JQCQ01000003.1.
DR AlphaFoldDB; A0A0R2NJY1; -.
DR PATRIC; fig|480391.4.peg.983; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000051249; 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; 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:UP000051249}.
FT DOMAIN 4..476
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 503..797
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1236 AA; 141743 MW; 66286CA72C7A36B9 CRC64;
MAKREYTVSQ KKAIYDHGSN ILVSASAGSG KTSVLVERVI QKILAGENVD QLLVVTFTEA
AAKEMKERIR VAITQQISQS DNHEQKQHLI DQLTRLGKAQ ISTIHAFCLS IIRSYYYVIE
LDPSFRIMTD TTESELLKEE VWNELREELY DIDGEVFAKL TQNFSGDRRD DSLRDLVLNL
FEFANANPDS KKWLEQMGSN YELDGDLMDS PFFKNKLIPG IKDQLQTIYK KALSLKDIAD
QGSELIAKSR DVIDEEVSEV QSVLDNGFGS DWNHLRTAML SVNLTGRLSA ARKDEVKEFN
QIANEIRSDK VMGYRVLFNN LVNDYFKLPE DMLLNAVQDS KNLIDELIRV VTMFSDRFKS
EKLERHSLDF SDLEHFALEI VTNESDAGRA VRHSFQKNFN EIIVDEYQDI NPLQETLLSS
VASTNPGNMF MVGDVKQSIY AFRMADPGLF LGKNDRFKDS DNPDERIILA ENFRSMRNVD
NFTNLIFNQI MDSKIGEIEY DDDAQLQYGA KYYPDEIKNK TEVLVYDEQK KQETDGPSLS
QTDGQITMIA QKIRSMIRNQ ETIFDRKEQV ERPVQFGDIV LLSQTRSKNL KIVEIFKQFD
IPIEVSDAQD YFQTTEISIM MDMLRIIDNP YQDIPLVAVL RSPMVGMNEN ELAFLRINQK
TGDYFESLLH FEKSFKVDLE NEFQANLKQK LDRFMQQLRK FRKLAQQANL VDLVWAIYND
TGYLDYVGGM PDGPQRQNNL HALYDRAKAY EESSFKGVFQ FVRFVEKMRD KKKDLAENPV
KTSEESVSVM TIHGSKGLEF PVVFLIDANH GFNKQDQNRP YILDRNEGVG ITLNDYVNHL
SIDTPQKIEI KDTLQKRSLA EEMRVLYVAL TRAEQRLIIT GSTDDAEKAL TGWSRALRSE
NDLLDDPVRE KAGHYLDWIG SSIVRIPAIA EQYNLEPAHT IEFDGEVELS FVNTEDLNQN
IVVDSSTNNE VPAVFNSDKT LEVPTDAQWI NEVLNFKYRD DVATRTTAYQ SVSEVKRIFD
DPDKLEMNFS EVTNEQQLKT VNRFVNKTLP SPKFLENVRK PKPTEIGTAT HLVLQEIDLH
QAVNEDVIQH LINDLVNNQV LAEEVAQSIN IENILRFFES DMGQLMLAHP DEVQREAPFS
MLVPAQTIFH EVKSQDDILI HGIIDAYLRI DGRVILLDYK TNFVKPGTKE AGVAKIIDKY
RGQINLYGLA LENITQQTVT DKYLYLLSVG ELVNVE
//
