ID A0A2A7MD48_9CLOT Unreviewed; 1250 AA.
AC A0A2A7MD48;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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:PEG29028.1};
GN ORFNames=CQ394_20500 {ECO:0000313|EMBL:PEG29028.1};
OS Clostridium neonatale.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=137838 {ECO:0000313|EMBL:PEG29028.1, ECO:0000313|Proteomes:UP000220840};
RN [1] {ECO:0000313|EMBL:PEG29028.1, ECO:0000313|Proteomes:UP000220840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LCDC99A005 {ECO:0000313|EMBL:PEG29028.1,
RC ECO:0000313|Proteomes:UP000220840};
RA Bernard K., Burdz T., Wiebe D., Balcewich B., Alfa M., Bernier A.-M.;
RT "Effective Description of Clostridium neonatale sp. nov. linked to
RT necrotizing enterocolitis in neonates and a clarification of species
RT assignable to the genus Clostridium (Prazmowski 1880) emend. Lawson and
RT Rainey 2016.";
RL Submitted (OCT-2017) 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}.
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:PEG29028.1}.
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DR EMBL; PDCJ01000006; PEG29028.1; -; Genomic_DNA.
DR RefSeq; WP_058293217.1; NZ_PDCJ01000006.1.
DR AlphaFoldDB; A0A2A7MD48; -.
DR STRING; 137838.GCA_001458595_00210; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000220840; 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; IPR016137; RGS.
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; PS50132; RGS; 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:UP000220840}.
FT DOMAIN 4..477
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 518..822
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT DOMAIN 1124..1247
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1250 AA; 145193 MW; C4A17B69E74C99D0 CRC64;
MGETKWTNEQ LSAIKTRNCN LLVAAAAGSG KTAVLVERII KIITDEENPV DIDKLLVVTF
TNAAAAEMRE RIANAISKAL DENPDSKNLQ NQLTLLNRAN ITTMHSFCLD VIRNNFHKID
LDPSFRIGDQ TETILIKSDV IEELFEDRYD NDDQEFIDLV EAFSSYKSDD NLKELILNLY
NFIMSAPWPE MWLKESTEAF NISSLDELNR SKWAEVLINS IKVEVEGYIK MYDKAIDIIN
HTDGLEGYLD NFIDEKEYLE RIYKLENNNL EEIYTLLTDI KFQRLKTIKK DKISDEDAQG
IVKKIRDDIK KKITDLKDNA FSLMPKEMIE SIQGAYPYVK KLSEIILDFG ERFSKKKKER
NILDFNDLEH LCLKILIDHD EDNNIIPSQV ANDFREFFDE VLVDEYQDSN NVQETIINLV
SRKELNNPNV FMVGDVKQSI YRFRQANPSL FIDKYNTYKI NEGLNRKIQL YKNFRSRKEV
IDGVNYIFKE LMSDTVGELE YTEEESLNLG ASYEISNDES ITLGGPIEVN IIGKKDDNIY
KDTEEHDESI IDDSDAEITG INLEGKIIAK RIKELMSSNN ESKFMVLDKQ TGEYRPLKYK
DIVILLRATK NYSEVLLEEL GEEGIPVYAD TGSGYFESIE IRTIMSLLKV IDNPLQDVPI
LSVLRSPIMG FTAEELTDIR LQDKEKYFYE NILCIAGKYD EKSDKVYSDK LIEKCNYFIE
KLTEWREKVI YTPIDEFIWM LYMDTAYYGY VGAMPNGVLR QANLKILFQR ARKFEETSFK
GLFNFINFIN RLTRSSGDMG SAKILGENED VVRIMSIHKS KGLEFPVVFL CGAGKNFNLM
DLNKSILYHH ELGFGPDFID LEKRLSLGTL AKEAIKKKMR LETLSEEMRI LYVALTRAKE
KLIITGCVND IEKSIEKWFN ASILDKNIIL PSEVLKGRSY LDWIGIALCK HNDGNILRER
IAVSNEFSKD DSSSWKINII SKNELLNEKE NEEVAEENEL TIKKDEINKE LYEEISSRLG
YKYPYELATT IKSNISVSDL KKKNIEETVD IEEIFIEKEP LIPKFLQEEK GLTASEKGTI
VHLVMKKLNL DKVDSAEDIK LQIGNMVSDE ILLEDEAKVV RVNKILKFFN NPLGKRMIEV
YKNNPNKLYR EVPFYTEISS IEVNNELSEE YKNENIRLQG IIDCFFEEED KVILIDYKTD
YIEEEKEDEF KNKYIKQLEY YSNAIFKIIG KKVDEKYLYS FYLDKYIRLR
//
