ID A0A1M4YNB0_9FIRM Unreviewed; 1185 AA.
AC A0A1M4YNB0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=SAMN02746064_01824 {ECO:0000313|EMBL:SHF07294.1};
OS Alkalibacter saccharofermentans DSM 14828.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Alkalibacter.
OX NCBI_TaxID=1120975 {ECO:0000313|EMBL:SHF07294.1, ECO:0000313|Proteomes:UP000184251};
RN [1] {ECO:0000313|EMBL:SHF07294.1, ECO:0000313|Proteomes:UP000184251}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14828 {ECO:0000313|EMBL:SHF07294.1,
RC ECO:0000313|Proteomes:UP000184251};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FQTU01000013; SHF07294.1; -; Genomic_DNA.
DR RefSeq; WP_073271261.1; NZ_FQTU01000013.1.
DR AlphaFoldDB; A0A1M4YNB0; -.
DR STRING; 1120975.SAMN02746064_01824; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000184251; 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; 3.90.320.10; -; 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|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:UP000184251}.
FT DOMAIN 2..458
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 489..775
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 23..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1185 AA; 136424 MW; 93EB903548958E65 CRC64;
MADWTKAQER AIESREKSLL VSAAAGSGKT AVLVERIIRL VVDDRVDVEK LLVVTFTKAA
AEEMKQRISS TLVKKMSEAT GEERGFINRQ INALPFASIS TIHSFCSSVV RRYYHVIDID
PALKVGNETV LLILRQRAME ELFEQEYEQE DEEFIKLMES FGNDRRDDRL REMVEKVYGF
LMNRPDPKAW GRKVVDSFGV DMQGFDRGSY YVFFAQSTKV KLEHAALLLT RALEDLKGTD
NFEKTSAVVQ DELNNVKALI NSLENGFSAF RKVLDSVGFA RLIIKTEDAD LKEKIKQSRD
EAKDIAKKLI EKFGYEDAET MVENLNEMKS RAAFLIKMAE RFEEIYSRMK REKSIMDFND
LEHFCMKILA NDEVANQLRE EYRYVFIDEY QDSNQIQDVI ASRIQRENNL FLVGDVKQSI
YRFRLSDPTL FIQKSLVYES ADSSINELLH LNTNFRSRST IIDFINYVFE RTMCSYVGEM
DYTEKEKLNP GLILPEMECD KTEIYLISND LEKDDSEEEE EIEEMKLEEL EAKVIASKIK
SLMGTEIFDA KKQEYRKLGY RDIVVLLRTV KKKGQIYQEV LMENGIPVYA ESGTGYFDTL
EISLLLDVLR VIDNRRQDIP LLSVMRSPVF KFTIDEIISI REAAKGKSMV EALLKASENP
EEALQEKAQG MLSVIARWKK QSRVMPLDRF LWSILVETDY YGYVGALPGG VQRQANIRML
VDRAKEFADS SMKGLFNFVK FVEELKNTKT DLTGAKVLGA MDDVVRIMSI HKSKGLEFPV
VFVGGMNKNF NMLDIQQSLI LHKDLGLSME YVNLDERRYC ETIYKSIAKE KTALEVLSEE
MRVLYVAMTR ARDKLIMVGS GKRLDSKIEG WAKPLSAYTV SKAKTYLDWV LGALLGYEEA
IVLAKQGAYE SEMVKIEKIS MDSIARVESE QDRYINKISD YFAALEDTTG QVPPQIIERL
EWSYPWEREI TLPSKMSVTD MKRFKRTKNL IKTSEELKTP IFLQREKTKK ASEIGSANHF
VMQHLNLERI KHSGDMADEI NLQLSGLFKS ERLDVSFEGK INVGAIVAFF ANTLGKRMIE
SPKIYREQTF NLEIKESELY EGGSPDESVL VQGMIDCFFR EENHWILIDY KSDYFASEKQ
KADILDKYKD QIAVYAKAIE KITGKRVKES YLYLLHSNEA LPVTT
//
