ID A0A0R2MRF5_9LACO Unreviewed; 1262 AA.
AC A0A0R2MRF5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=IV64_GL000426 {ECO:0000313|EMBL:KRO14747.1};
OS Lactiplantibacillus xiangfangensis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=942150 {ECO:0000313|EMBL:KRO14747.1, ECO:0000313|Proteomes:UP000051783};
RN [1] {ECO:0000313|EMBL:KRO14747.1, ECO:0000313|Proteomes:UP000051783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 26013 {ECO:0000313|EMBL:KRO14747.1,
RC ECO:0000313|Proteomes:UP000051783};
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:KRO14747.1}.
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DR EMBL; JQCL01000007; KRO14747.1; -; Genomic_DNA.
DR RefSeq; WP_057705221.1; NZ_JQCL01000007.1.
DR AlphaFoldDB; A0A0R2MRF5; -.
DR STRING; 942150.IV64_GL000426; -.
DR PATRIC; fig|942150.3.peg.437; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000051783; 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; 1.10.274.50; -; 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}.
FT DOMAIN 5..482
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 524..820
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 535..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 26..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1262 AA; 143098 MW; F6650BB191B4D362 CRC64;
METKTQYTDS QKAVISQQGN NLLVSASAGS GKTTVLIERI MRKIMAGTNI DQLLVVTFTN
LAAKHMKQKL ESQLNKRISQ FLTDHPGQTT ASPEVRQFRQ QLNLLGVANI STLDAFCLRV
IQRYYYVIDL DPVFRLLTDN TEGLLIRDQV WDTVRESLYE KDGELFDLLT ANFSNDRSDD
GLGQLVFRLF DFAQSTPDPE AWLKQLVTNY KLQGDSLTAT PFYQEKLLPL LKTEFETMVN
RMDQAVKIAT EADLAPKTIE ALQVAQRDLG TMISDLDNTD WNALRAATAS FKVGRLTKTY
KDDPEKTSRA KAMGTLVDGV KKQMGSIGET YFAADEQQVL DVMAGAAAIV QELVRATLCF
KEAFAKEKRR RHVLDFSDLE HLTLAILTNT SESGQGALTQ LRAQFEEVMV DEYQDINSLQ
ESILQLLARK TPGNMFMVGD VKQSIYQFRL ADPLLFLAKY RDFGKHPEHG ERIVLAENFR
SVENVDRLTN LIFSQLMDAP VGQIEYDQAA YLKYGPKDYP ADMPQTTSLL LYQTDDDQPE
KTPVRGSQPD SDNEESNFSI DDPSIGSITM VAQKILALKK MDHPIFDRST GKYRPFHYSD
AALLVPTRNH NLTIIDIFKQ YHIPIVVNDA QNYFQTTEIR IMMALLSIID NPYQDIPLVA
VLRSPIVGLD ENQLVYLRIQ NKTSDYFQAL RDFYQTYPTK GNPSAYGDQL YAKIEVFMQQ
LTAFRDLARR NQIVTLIWQI YEQTGFLDYV GGMPAGQQRQ ANLHALYERA YTYEQGSFKG
LFQFVRFIKR MQEKDQDLAS AVAETDTEAV SVMTIHGSKG LEYPVIFLMD MDKRFNQTDT
RANALMDRDA GIGINYLDPE HRVKYPTLPR LVIQQVVSQK LRAEEMRKLY VAITRAQQQL
FLVGTITSID VATEKWRQGF SSDGRVLSTL ARVSTNNQLD WVGMALMRHP LMKAYWGDEW
PTYSLEGDQT KFTLELGDAS SIGQRKQVAG TDEQLSAVDQ VEQTVDVDVD QMTRDELTNL
LNFKYVHQAS TVTTAYQSVS EVKRLFEDPD DAQMNTNPTV SAQHAKPTSR FVTGDLAVPQ
FLQTTQEPTS AEVGSATHLV LEQLDLTQTI DETTVQATID DLVAKQVLTR EVAQLIRIDA
IVGFYTSDLG QRILADPTKV HREVPFSLLL PARQLFDELD EHEHAKILIH GIIDGYLETA
DGLILFDYKT DHVKQPQDLL TRYAGQVELY AAALRSMYQR PVVQQYLYSL PQRTFVPVTK
KK
//
