ID A0A0R1P5J2_9LACO Unreviewed; 1287 AA.
AC A0A0R1P5J2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=FD27_GL000611 {ECO:0000313|EMBL:KRL27869.1};
OS Limosilactobacillus frumenti DSM 13145.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=1423746 {ECO:0000313|EMBL:KRL27869.1, ECO:0000313|Proteomes:UP000051445};
RN [1] {ECO:0000313|EMBL:KRL27869.1, ECO:0000313|Proteomes:UP000051445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13145 {ECO:0000313|EMBL:KRL27869.1,
RC ECO:0000313|Proteomes:UP000051445};
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:KRL27869.1}.
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DR EMBL; AZER01000014; KRL27869.1; -; Genomic_DNA.
DR RefSeq; WP_057749976.1; NZ_AZER01000014.1.
DR STRING; 1423746.FD27_GL000611; -.
DR PATRIC; fig|1423746.3.peg.620; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000051445; 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:UP000051445}.
FT DOMAIN 4..484
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 512..814
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 1287 AA; 147694 MW; EBC9AD2A908BC417 CRC64;
MAEFKPTPAQ QQAINDRHQN ILVSASAGSG KTAVLVQRAI GLIKEGIDVN RLLMVTFTDA
AAKNMRDKIR AALQKEATAA TNSVAMKRAM AKQMNLVATA DISTIHAFCL KLIKRYYYLI
NLDPQFRLLT DDTERLLLQE DTWQQFSEHL YANADYQADD RASFHELVLN FSRDRDDTGL
DDLVLRLSKI ANAQPDPEAW LRQLPEHYFL GNSDITESKF FVNDLEPLVA EQLEQLINDS
HELVLRMQDT GYEKPSAVLT ADQELLQQLK DELTNCTWDQ LRAHFQGAKF KRLAGGPTKK
DAGTPEYEDY QAIKADRDRI KKQLRQLSEH FFIYPAAQLK SLSQKSQALV AELVNVVIGY
RQQYQQVKLN RHVLEFNDLE HYAYQILTPP ADDADWQALV ADLRNHYREI MVDEYQDTNP
LQEGILKKLA SPERHNMFMV GDVKQSIYRF READPSLFTD KYQRYQQDGA AGEDIVLAEN
FRSMRNVVDF TNLLFEQLMD RQVGQIDYDE DAHLKYAATY YDEDEQNQPR PTELLLYDAN
VDPDQPTEDD KLTGELQMVG MRIKQMIAHQ EQIYDSNLRR MRPINYGDIV ILERTKGINN
TLMEQFNKLN IPLTVHDVES YFQATEVRVM MALLKVIDNP HQDIPLVAVL RSPIVGLNNK
ELTMIRLQNR SADYYSACRE FVDNYDQHSV QRRSLLPEDA INDLATKLKR FLADLNEFDQ
TAQQQTLVDL IWQIYQRTGY LDYVGAMPGG QQRQANLHAL YERAQNYEQT SFKGLYQFTR
FIEKMQEHDQ DLGVAPAQLA ENTVNVMTIH GSKGLQFPIV FLIDATHGFN NSTSKENAVT
DADAGLGIRY MDEHRLVYDT PQRQVILEQI QRSERAEGLR VLYVALTRAE QRLIITSSFN
EQRRNQKLAT AWERWQKAFQ SDQQVLGAQV RVNANSFMDW IGLACARYRQ FFKPEDVAVN
VAGKEGMNLL PSPLDHDQAY PWMQNQAVFK VLSFSQQQVN DALAQLNQAA ADSDHEVEPI
DPDLKNHFAD VLSYQYPHQV ATQTTAYQSV TDVKRVFEDP DNRQMGQWDY DDQRKTKHRG
VYLKNDFATP RFVQQTDQSP AAAEVGTATH LVFQKLPLDK NTVDHNLVAN TIDKLVDQQL
IAPAVAHQID QEGIVAFFAT AIGQQILNDP TNYQREAPFA MLMNGHELFR DVQAQDDERI
LIHGIIDGYL EQPTGITLVD YKTDHVNTNN TAASIERIKD RYRGQLELYR QALNMMKEEP
VVQMGLYLVE LRKFISFSIG GKTGADH
//
