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Database: UniProt
Entry: A0A0R2A7E7_9LACO
LinkDB: A0A0R2A7E7_9LACO
Original site: A0A0R2A7E7_9LACO 
ID   A0A0R2A7E7_9LACO        Unreviewed;      1232 AA.
AC   A0A0R2A7E7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=FC26_GL001408 {ECO:0000313|EMBL:KRM62703.1};
OS   Paucilactobacillus vaccinostercus DSM 20634.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Paucilactobacillus.
OX   NCBI_TaxID=1423813 {ECO:0000313|EMBL:KRM62703.1, ECO:0000313|Proteomes:UP000051733};
RN   [1] {ECO:0000313|EMBL:KRM62703.1, ECO:0000313|Proteomes:UP000051733}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20634 {ECO:0000313|EMBL:KRM62703.1,
RC   ECO:0000313|Proteomes:UP000051733};
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:KRM62703.1}.
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DR   EMBL; AYYY01000002; KRM62703.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R2A7E7; -.
DR   STRING; 1423813.FC26_GL001408; -.
DR   PATRIC; fig|1423813.3.peg.1434; -.
DR   Proteomes; UP000051733; 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:UP000051733}.
FT   DOMAIN          4..471
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          483..794
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   1232 AA;  138657 MW;  D44166BED7D9EAFC CRC64;
     MSKTHFTVTQ QQAIDDQGQN ILVSASAGSG KTSVLVERVI QKILGGESID RLLVVTFTEA
     AAKGMRDRIG QALKEAIAQT NTTDVKQHLK NQLNRLAVAD ISTLHAFCLH LIKQYYYLIN
     LDPQFRLLTD ETEGILLREN VWNDVRETLY ASGDPAFEQL TRNFSSDRSD DGLTTVVNQL
     DSYATATPRP HEWLAQLPTT YAVGGGPLIE TAMYQQQVLP ALVDVLQQIE ADLADALHQA
     GGDGFEKVQA VLEAELEQAK TAEKLVGSAS WDDCRQFLQA LKFSTLRGPK DDEAKATFES
     IKELRNNAKK AINALAPHYF ALDEATTKQI SSQAEQLVTT LVDVVERYRA AYQAEKQRRH
     VLDFSDLEHY TLQILTTATP DGQAVVAQLR DHYHEIMVDE YQDTNQLQES ILQTLVNDDP
     GNMFMVGDVK QSIYQFRQAD PSLFLRKYTT YRQPESTDGE TIVLAENFRS VNNVTDFTNL
     IFQQLMDTQV GEMDYDEDAH LKYGATDYPD RGVPTEIMLY DSTTEPTALD QKLPLLEAGD
     KLTGEIQMVG LRIQRMIEQH ELVYDRKAQQ MRPISYGDIT LLSATKNNNN LIVEQFSQLG
     IPVTVRDAQN YFQATEVRIM MALLRIIDNP YQDIPLAAAL RSPMVGLDEN ELAYLRIQDK
     TDEYFAAVTK FARATPKDAF AEQLQVKIRR FLDQLTKFRT IANQNRLVDL IWAIYDETGF
     LDYVGGMPGG KQRQANLHAL YQRAAMYEQS SFKGVFQFVR FIEQMQKRNK DLAQAPAQTS
     SDTVSVMTIH GSKGLEFPVV FLIDATHQFN MESLRQDCLL DAHAGIGVTY LNDENVKVAT
     LQKQIVKDTI QNKSRAEEMR VLYVALTRAE QRLIIAGAYK DANKAIANWQ RAFQSSGMLL
     PNQQRAQATN FMDWIGMSLV RHPQFDQNLL TDPQPWYGLG KDQTTFTVQV VTAADLQQDA
     ADEPVGVPSI DEQIETATDG QLSSAEQQAV LQVLNLQYDY QAATMTTAYQ SVSEIKRLFD
     DPDNQELIQI ELNPQARSEG RYVKSEFGQP HFMQQEQTAT PTQIGTATHL VLQTLSMATR
     PDATAISQVV TRLQLNNIIS PEVAQKINQS QIEAFFDTPL GQALLTHADS LQREAPFSML
     LRGDQLFTQL TADEKILIHG IIDGYFETAD GLVLFDYKTD HVKGDNPVAI QQVVDRYRGQ
     VNLYARALTS IKHQKVAHKV LYLLDIGKMI EV
//
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