ID A0A371J9C1_9FIRM Unreviewed; 1232 AA.
AC A0A371J9C1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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:RDY29287.1};
GN ORFNames=CG710_018660 {ECO:0000313|EMBL:RDY29287.1};
OS Lachnotalea glycerini.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lachnotalea.
OX NCBI_TaxID=1763509 {ECO:0000313|EMBL:RDY29287.1, ECO:0000313|Proteomes:UP000216411};
RN [1] {ECO:0000313|EMBL:RDY29287.1, ECO:0000313|Proteomes:UP000216411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCRI-19302 {ECO:0000313|EMBL:RDY29287.1,
RC ECO:0000313|Proteomes:UP000216411};
RX PubMed=29051240;
RA Maheux A.F., Boudreau D.K., Berube E., Boissinot M., Raymond F.,
RA Brodeur S., Corbeil J., Isabel S., Omar R.F., Bergeron M.G.;
RT "Draft Genome Sequence of a Sporulating and Motile Strain of Lachnotalea
RT glycerini Isolated from Water in Quebec City, Canada.";
RL Genome Announc. 5:e01059-17(2017).
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:RDY29287.1}.
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DR EMBL; NOKA02000070; RDY29287.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371J9C1; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000216411; 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};
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|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:UP000216411}.
FT DOMAIN 3..472
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 500..802
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 24..31
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1232 AA; 142900 MW; 70134CBCA5DFA3CA CRC64;
MSVAWTSEQQ KVIDLRNRNI LVSAAAGSGK TAVLVERIIA MITDSNELLD IDKLLIVTFT
NAAAAQMRER ISEAIEQKLE ETPSNSHLQK QATLVHNAYI TTIHSFCLRV IRNHFNRIDL
DPSFRIGDEG ELKLIKSDII EKILEKHYKE KSDEFFHFVE SYSTGKSDKE LEDMILQLYQ
FAMSYPWPKE WLIQCKNSYK LTSIQELEQT PWYQNIVDNI MVIVKELMEQ LNHLIELAVS
TDGPYMYEET LKNEKEMLSN LLHLDSYMDY YTQFKAISFG RLSSKKDETV SGNLRELVKK
QRDGIKKTVS SLSERYFYDS PEQILQDMQK CSNSIDVLVD LTIEFIEEYK SAKIDKNLVD
YNDLEHFALN ILVEKSNDNW FPTEAATEYQ EIFEEIMIDE YQDSNLVQEM ILRAVSRERM
DKHNVFMVGD VKQSIYKFRL ARPELFMEKY NTYSLTDSAF QRIDLDKNFR SRIEVLDGTN
YIFNQIMTNT LGGIEYNNEC ALYLGANHPE PEKENDYEAE LIVIDLDSTK IEDENNMKIS
LLDTKDYTAR ELEAKAVAAR IKELINHEHG LKVIDKGTKK YRVACYSDIV ILLRTMSGWA
ETFTSVLMSE GIPAYTGSST GYFSTIEVTT LLNLLRIIDN PLQDIPLTAV LASPIVNLSG
EELAVIKSSY KQADIYEGCR QYSLEGKEEF LKQKLYDFFT RMEQFRKMAV YTPIHELIWF
ILDKTNYGRY VATMPGGEQR KANLDMLVEK AIAFESTSYK GLFNFVRYIE NLQKYDVDFG
EAEIANENDN TVRILSIHKS KGLEFPIVFV SGMGKAFNNQ DSRAKLIMHP DLGIGADYID
FEHRVKAPTL IKKAIQKELQ MENMGEELRV LYVALTRAKE KLILTGAMSK LKNKLLGYSQ
NLNDKEKLSF RSISEASNYM EWVLQAVIRH KDSIELLRKY ELEENFCELL FAKNAKYAIR
VIELSDLVKE EMVAQITNQD IKDDLLRGLL DREENEQIQK QMEERLNFVY PYEKIKNIHT
KMTVSELKRM GQNIDEDTSM PIILEEIPVP LLPKFLAEEG TLTGSDRGIA YHKALQLLDF
KSIETTEDIE NQLNKMLEEH KMSKEAGESI DISKIERFLH SEIGERMIRA DLFGKLYKER
PFVIGVKVNE LNNDLDSQDM ILVQGIIDAY FEEGEEIVLV DYKTDYVRTE KELTTKYKAQ
IEHYQGALMR MTQKNVKEKI IYSLYFDKSI YL
//
