ID A0A1S9I4V8_9CLOT Unreviewed; 1279 AA.
AC A0A1S9I4V8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=BS638_08965 {ECO:0000313|EMBL:OOO65258.1};
OS Clostridium tepidum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1962263 {ECO:0000313|EMBL:OOO65258.1, ECO:0000313|Proteomes:UP000190256};
RN [1] {ECO:0000313|EMBL:OOO65258.1, ECO:0000313|Proteomes:UP000190256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IEH 97212 {ECO:0000313|EMBL:OOO65258.1,
RC ECO:0000313|Proteomes:UP000190256};
RA Dobritsa A.P., Kutumbaka K.K., Werner K., Wiedmann M., Asmus A.,
RA Samadpour M.;
RT "Clostridium tepidum sp. nov., a close relative of Clostridium sporogenes
RT and Clostridium botulinum Group I.";
RL Submitted (DEC-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}.
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:OOO65258.1}.
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DR EMBL; MRAE01000020; OOO65258.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9I4V8; -.
DR STRING; 1962263.BS637_06200; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000190256; 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}; 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|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 4..499
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 534..853
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT COILED 284..322
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1008..1035
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1279 AA; 150429 MW; 501E87303AC8FDDF CRC64;
MSSTNWTDEQ RQAIFTKDCN LLVAAGAGAG KTAVLVERII QKILDKEEPI DIDKLLIVTF
TNAAAAEMRE RIGDAISKAL DENPESKILR KQFTLLNKAN IMTIHSFCLQ VIKNNFHTIE
IDPNFRICDE TEGILMKQEA IDELFDELYE FENEDFINLV ESYASRKDTR LQELVLELHR
FAKSAPFYKN WLLNMAEEFN VGENFNFEET SWADMIMEDM KILLHGFKNM LHQSIDIILN
SQGIDYYYEP FKMDLNFINS LLKKSNFKDF RNEIINYDFP KLPAKRNKDA DKEAKERVKK
LRDKVKKKIV ELKNILDSYE NEFIKREFMF LYPSMKALSN LVILFDKKYE AKKRERDLID
FNDIEHLCLA ILTDKDEEGH IIPSNIALDY RRKFEEVLID EYQDSNLVQE VIMSMVSRVK
GYWSFYNGQL IFNEQKINLE EPQRGLDIPN RFMVGDVKQS IYRFRQAKPE IFLEKYNNYN
EKQGSKHRKI KLFKNFRSRE EVINGVNYLF KQIMSKTIGE LDYTEKEALS IGASYGEEVK
GEPIELCLMD KKYEISQEAL KEYNIDEEEA LDNIQIEGRL VAKKIQELIG NELEGGLKVF
DKKLGEYRRI QYRDIVILMR ATSNWAPVFV EEFAKEGIPV FADINSGYFD TTEIKTIISL
LQIIDNPLQD IPLLSVLRSP IASFTDDDLI DIRMVNKNIA FYECMEIIYR LYKNESLDSY
YSFYIENEDK VNKIVKDMKE EVKNKICSFI DKLNLWRKKS IHVNIDEFIW FLYVETGYYG
YVGALPAGEQ RQANLRILFQ RAKQYENTSY KGLFNFINFI NKLKFSSGDM GSAKILGENE
NVVRIMSIHK SKGLEFPVVI LSGTGKNFNM TDLNKNILFH RDLGYGPDYV DIERRIAYPS
LVKNIIKNKI RLETLSEEMR ILYVALTRAR EKLIITGLVN NIDKTVESWL NLSEDKNKVP
EYAVMNGKTY LDWIGPAVIK HKDAISFRKE INMMSELSNI VDDKSKWKIE LYNKKELLKE
KVEEDEVEIS EKIKETLMKL EESNYKEEIY IRLSFKYKYD NASNIPAKLS VSDVKKEFIL
DDKENTEELF KKVELRKPTF MEEKKKISST ERGSIIHLFM QHLDLKSVKN EDIIKDQINR
LIEKEFITYE QSKVINPYKI LKFCKSELGQ RMINSNNINR EMPFFIEIPA LEIYKDLDKE
IYKDEKLIIQ GVIDCCFEED DGLVLLDYKT DYVTDIEEIK NKYKMQIQYY EKALNKITGK
TVKEKYLYLF SIDNYVKMD
//
