ID A0A081BHE9_9LACO Unreviewed; 1250 AA.
AC A0A081BHE9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
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:GAK47467.1};
GN ORFNames=LOSG293_070060 {ECO:0000313|EMBL:GAK47467.1};
OS Secundilactobacillus oryzae JCM 18671.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Secundilactobacillus.
OX NCBI_TaxID=1291743 {ECO:0000313|EMBL:GAK47467.1, ECO:0000313|Proteomes:UP000028700};
RN [1] {ECO:0000313|EMBL:GAK47467.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG293 {ECO:0000313|EMBL:GAK47467.1};
RA Tanizawa Y., Fujisawa T., Mochizuki T., Kaminuma E., Nakamura Y., Tohno M.;
RT "Draft Genome Sequence of Lactobacillus oryzae Strain SG293T.";
RL Genome Announc. 2:e00861-14(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:GAK47467.1}.
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DR EMBL; BBJM01000007; GAK47467.1; -; Genomic_DNA.
DR RefSeq; WP_034526803.1; NZ_BBJM01000007.1.
DR AlphaFoldDB; A0A081BHE9; -.
DR STRING; 1291743.LOSG293_070060; -.
DR eggNOG; COG1074; Bacteria.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000028700; 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; 6.10.250.2380; -; 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};
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..470
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 509..800
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 1250 AA; 142181 MW; B6EFA9ECD33EC83D CRC64;
MADIKYTKSQ QQVIDTRDTN LLVSASAGSG KTRVLVDRVI KRITEEGIGV DQLLIVTFTK
AAAKEMKDRI HKSLERKITE TTGENRRRLM HQLSLLPVAN ISTLDAFCQQ IIERYYYIID
LDPVFRLLAD KTEGILLRDQ VWQDVRETLY ENDEDGSFKR LTANFSNDRN DDGLTDLVNR
VYFYANAKPN PAQWLQQLAD PYVINGTLND SDLYRKQILP LIQNRVEQAI KDLGYALEKA
NQAEFPKLAE LCETEMASLR ATQDQLPDLK WDEVRETLFV KRSTSPRVTK KDDVPELKKE
AQEARKAALA VIDELQDTYL ALNEAITTEV MQQSHAIVTK LATTVQAFSD AYQQEKLRQH
VLDFSDLEHY ALEILSADTE QGKAVREQLR DRYEEIMVDE YQDTNALQEA ILQTITRHEP
GNLFMVGDVK QSIYRFRLAD PSLFVGKFNH FGEDPQAGKD IQLAENFRSI KNVDDFTNLI
FTQLMNQELG EMDYTGGAKL VFGASYYPDG YTPATELLIY EDQQTNVMTE QNEDEPIDAT
FKIDDKVRGQ VAMVGQRILE MQANGTEIFD RETGEMRPVA FKDFALLTPT KNNNLVITEL
FAQMGIPVLV NDAQNYFKTT EIQIMMALLS LIDNPYQDIP LAAVLRSPIV GLDENQLAYL
RVTDKTGDYF QAVLQFHDTY QSGNPYGDAI FPKIDRFLKQ LTIFKDVAKQ NQLVELIWRI
YQETGFLDYV AGMPAGKQRQ ANLHALYERA AVYEKSNFKG LFQFVQFIQR MQSEDEDLAE
APTEVSDDAV RVMTIHGSKG LEFPVVFLMD MSHQFNMSDT KGDAVLNDKL GIGITYFDEH
RRAKFDSLQK MLASEATKQA SLAEEMRKLY VALTRAEQRL IIVGTVKDRE KAVANWEKAC
QSDRLVLDMN DRLNTNNALD WIGMCLVRHP RFAESLRSRQ VDPHFIDLNG DETQFQIEFV
TVTDLQKIGQ QTTPMTGAEW LKTLHNKLGD ADYSEVNVSD IDRVMNFSYP NLQATQTTAY
QSVSEVKRLF NDPDTIEMGD FSINQNETGA ANRFVAKDFD QPRFLQTKQA PAATEIGTAT
HLLMQEIDLT QPITAARIAA RVQELVMGNV LTEEVAAKID QASVLNFFEN SELGQLLVAH
PAQVKREQPF SLLLSAQKLF GEIDDEEAKV LIHGIMDGYV VLPERVILYD FKTDYVAFND
KAASIEKIKE RYRGQVNLYA EALADILDRP VTDKYLYLLA SGDLVTIEGE
//
