ID E3C8N6_9LACO Unreviewed; 1386 AA.
AC E3C8N6;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
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:EFQ52918.1};
GN ORFNames=HMPREF9265_0567 {ECO:0000313|EMBL:EFQ52918.1};
OS Limosilactobacillus oris PB013-T2-3.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=908339 {ECO:0000313|EMBL:EFQ52918.1, ECO:0000313|Proteomes:UP000003070};
RN [1] {ECO:0000313|EMBL:EFQ52918.1, ECO:0000313|Proteomes:UP000003070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB013-T2-3 {ECO:0000313|EMBL:EFQ52918.1,
RC ECO:0000313|Proteomes:UP000003070};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (OCT-2010) 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}.
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:EFQ52918.1}.
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DR EMBL; AEKL01000059; EFQ52918.1; -; Genomic_DNA.
DR RefSeq; WP_003713253.1; NZ_AEKL01000059.1.
DR eggNOG; COG1074; Bacteria.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000003070; 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; 2.
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}; 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 4..586
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 616..930
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT COILED 330..357
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1386 AA; 156815 MW; 00E78519EDE7DA15 CRC64;
MADFKPTPAQ QQAISDRDQN IIVSASAGSG KTAVLVNRAV DLIKEGRATV DRMLLVTFTD
AAAKNMRDKI RQRMQEVAQA EPRLRDLMNE QVNRLAVADI STIHAFCLKL IKRYYFLIGL
DPQFRLLTDD TERLLLQEDV LHQVNEQFYA SADEESDDSA SFGQLVLNFS SDRDDQGLND
LVLKLMEIAN AQPDPEQWLA QLPTSYQLNG PVLDSAFYQR QLLPLVLQRL DQLRHDFAEL
TQRADQEGLS KAREVLEDDQ VILNQLQAAL DPAHLTSDQL QAILGGVSFG SFSGRPKKGA
AVYDDFKALN QERNQLKKEW PTVAATVADK DAALAQLDQF SARFQELRDR AAAAQLDDKT
LTSLDKDLQQ FAQARQLLVP DSWNAVRAII RGAKFRTMAG KPKGDPVAAD VYATLTASRQ
ALKKQLTGIQ DSFFAYDEDQ FQEISHQSQR LLTKLSQVTV AFRRAYQQVK LSRHVLEFSD
LEHYAYQILT PPADQPDWQE LVANLQRHYQ EIMVDEYQDT NRLQEAILTR LTNPDQHNMF
MVGDVKQSIY RFRQADPSLF LHKYQRYRQP GAGDEAIVLG ENFRSMSNVT DFTNLLFAQL
MGADVGEIEY DQAAHLKYAA TYYETADNQP RPTEILLYDA NADQGAIKES PDQHEDDKLA
GELKMVGMRI KQMVANEEQI FDPATQQLRP INYGDIVLLE RTKSINNTLM EEFSKLEIPL
TVHDVESYFQ ATEVRVMMAL LRLIDNPHQD IPLVAVLRSP LVGLSTKELA FIRLQNRSAN
YYGALQTFKS NYANADRHLI KPELLNATAT ADQPDPVAVL YDKVSHFLDQ LATFRQTAQQ
QSLVDLIWQI YNETGYLDYV GAMPGGAQRQ ANLHAFYQRA HDYEQSSFKG LYQFIRFIEK
MQEHDKDLGV APTQLVKNTV NVMTIHGSKG LQFPIVFLID ATHGFNQQAT RETAVVDAVN
KVGIEYTDPE EVRYDTPQRQ AIISAVQQGE RAEDLRVLYV ALTRAEQRLV ITGSFNEENR
RQNLASAWTR WQKAFQSPAT LLGPQLRVNA RSFMDWIGLA LARSTKFRVK QVAPTGMELD
ESAMADYQHY QPLFAGQRFT VGCYTAADVT EKLASLQEQQ EETVLTGQTA IDQEQLKQIK
QLLGARYPYQ VATKTTAYQS VTDVKRLFEY PDNAVEAQWD YEQQQREKQA QGIYFNNHFA
EPAFIKQADE QPAATTIGTA THLVFQKLPL TAGEVSPTLV ADEVQRLVDQ GLMTPAVAAK
INVTGVARFF QTAVGQQVLA VPEHYHREEP FAMVMNGAEL FKEIKTSDQE QVLLHGIIDG
YLETPTGIIL VDYKTDHLRP GFGEAEIVDR YRGQLNLYKE ALGLMKPLPV VQMGLYLVES
EQFITI
//
