ID A0A0R1UB75_9LACO Unreviewed; 1203 AA.
AC A0A0R1UB75;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=FC46_GL001880 {ECO:0000313|EMBL:KRL90623.1};
OS Lactobacillus kalixensis DSM 16043.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1423763 {ECO:0000313|EMBL:KRL90623.1, ECO:0000313|Proteomes:UP000051036};
RN [1] {ECO:0000313|EMBL:KRL90623.1, ECO:0000313|Proteomes:UP000051036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16043 {ECO:0000313|EMBL:KRL90623.1,
RC ECO:0000313|Proteomes:UP000051036};
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:KRL90623.1}.
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DR EMBL; AZFM01000008; KRL90623.1; -; Genomic_DNA.
DR RefSeq; WP_057798073.1; NZ_AZFM01000008.1.
DR AlphaFoldDB; A0A0R1UB75; -.
DR STRING; 1423763.FC46_GL001880; -.
DR PATRIC; fig|1423763.3.peg.1916; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000051036; 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 Gene3D; 3.30.160.800; -; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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 2..475
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 502..788
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT COILED 830..864
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 23..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1203 AA; 139548 MW; 7D56EA51A950D79C CRC64;
MPEYTKEQAK AIDYHGKDIL VSASAGSGKT TVLVQRVLKE ILSGIGVDEL LIVTFTKAAA
EEMKQRIKNE LTKAIRKENH KDRRIYLQRQ LNNVDTANIS TIDAFCLDVI HRFYYAADLD
PSFSILTDET QAALMKERAL REIEAETLEG KDSQEFEEFY NNFVGDRDNE TARGLLLDLY
NYAMAKPNYR QWLRELPNQY KIGDSLVNSD VWQKQIKPYL LATLKDLQNK IQRLLDEEIF
QTDKMAKQLD NFKLFFGKLN VCISDLDEDQ DYDSLRSDLQ NCRFTIRTAK SKKWDEDIQE
FFEETTKIKK EAQDTILSIF SQFFATGENE QLAAMKKARR ITQTIVKSEQ KLIDRFNQFK
REENVLDYTD MEQIAFQILS QDTSNSQLAR EFYQNKFKEI LVDEYQDINN LQEQIIQQIK
NEDFNHLFMV GDVKQSIYGF RQAEPSLFLQ KYHDYGDKEN INEERILLSD NFRSTEPVTK
IVNQIFTKVL SKDFGGIDYQ GEGQLIFGAN YYPKNLSQSS EILYHKKERN SNTSDDDSTD
NFSEIQMVIS RIKQFKKEKM QIFDAKSGQL RPFEYKDIAI LTRSRSNNLQ IMQEFAKNDI
PLFITDAQNY FQTFELTVIM NYLKVIDNPD QDIPLTTVLR SPIFNFSNKE LGEIRANNKT
SSFYNAVLDY VGKNNALSEK VKLFLNQLES LRSFATTHRI SELIWSIYER TNLLEIMTAL
PNGEQRRANL ESLYERASSY ESAGFKGIYQ FINFISRMRK SQKDLAQPLL SKEADNSVRL
MTIHGSKGLE FPIVFYVGLE HKYQKTDSQG DYVLTSDTLG LTIKRETDRL NSLVRSMAQI
QKSKQNLEEE ARILYVAVTR AKQKLILVAD IPNFDKDSET WSDKNNLSLT DKLSATNPLS
FVGPTLNFKK NLPTTVDSIT SSVDQNSEFL YINFDEINEE KVEKEKHTED NIEHSLLTKA
VTQLFDFKYP FADASRTNAY QAVSELNKSS DPDEKDLDNS KMIRSSNRYL QKIDTRPNFL
FDSNFTGTEV GTATHLILQY FDYTGDGSEQ QLDEEINTLI LQKKLDPSIV PSLKKDEILW
FVNSDFAKVF AEKPENLKRE VEFSMLRPVN KNIGQRDFSD KNAKILVHGA IDGYYIENDG
IILFDYKTDH IDLSNLDFEI EKLKTRYKEQ LQLYEDALND ISKQKVKSKY LILLSAKKVV
QID
//
