ID A0A1E8EY31_9CLOT Unreviewed; 1252 AA.
AC A0A1E8EY31;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-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 ECO:0000313|EMBL:OFI05457.1};
GN ORFNames=CLOACE_16860 {ECO:0000313|EMBL:OFI05457.1};
OS Clostridium acetireducens DSM 10703.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121290 {ECO:0000313|EMBL:OFI05457.1, ECO:0000313|Proteomes:UP000175744};
RN [1] {ECO:0000313|EMBL:OFI05457.1, ECO:0000313|Proteomes:UP000175744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10703 {ECO:0000313|EMBL:OFI05457.1,
RC ECO:0000313|Proteomes:UP000175744};
RA Poehlein A., Fluechter S., Duerre P., Daniel R.;
RT "Genome sequence of Clostridium acetireducens DSM 10703.";
RL Submitted (JUN-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:OFI05457.1}.
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DR EMBL; LZFO01000026; OFI05457.1; -; Genomic_DNA.
DR RefSeq; WP_070110655.1; NZ_LZFO01000026.1.
DR AlphaFoldDB; A0A1E8EY31; -.
DR STRING; 1121290.CLAOCE_16860; -.
DR PATRIC; fig|1121290.3.peg.1676; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000175744; 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; 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}; 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}; Reference proteome {ECO:0000313|Proteomes:UP000175744}.
FT DOMAIN 4..469
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 493..820
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT COILED 879..926
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 1252 AA; 147942 MW; D6831E40B2C6682D CRC64;
MKETQWTEEQ KKAIETRGCN LLVAAAAGSG KTAVLVERII RKTTNKENPI DIDKLLIVTF
TNAAASEMKE RIGDSISKAL DENPEHKQLQ RQLALLNRAN ITTIHSFCIQ VIRNNFHILD
LDPNFRVADD TETILLKDEV LDEIFDEKYE NEEEHSFFNL IECYAGKTDE KVKNMILNLY
NYSRSLPWPE KWLIEKTEEF NVKEDFDFSK SKWAYILLNN LKIYIKGIKN KLNKAINIIE
KEETLTPYLD TFKEDLYNVN SLIKEKSWYE LCNTFNNLNF GKLKRCGKDA DKSLQKKVKD
IRDEIKKDLK KIKEDIFLDM DKIPESLRKM YSIIKCLTSI VIEFHKRYAI RKKERGIIDF
NDIEHFCLEI LIHEDKYGNL VPTETAFEYK YKFEEILIDE YQDSNMVQET ILNSISKGNN
IFMVGDIKQS IYRFRQAKPE LFLYKYNNYS EEEGNLNRKI KLFKNFRSRE EVINSVNYIF
KQIMSKNIGE LDYNEGEMLN LGASYKEINK EKALIEEKIE LHLIDKSSLD NKEYKEENGE
ELDSIQLEAK MVVKRIEDLI SPEEEKKFYV FDKEIDNYRP IKYRDIVVLM RTTSNWSPVF
MEEMLKANIP VFADTNSGYF ETMEVKTILS LLQIIDNPMQ DIPLLSVLRC PVFSFKAEDI
IDIRLVDDRL NIYEIIKKIL LYKNSKQEGV LNIEDSDENI ENIMENKYLI NKLEDFMNKL
KKWREISIHK SIDEFIWYLY VDTGYYGYVG AIPGGIQRQA NLRVLFERAK EYEETSFKGL
FNFVNFINKL KNSSGDMGSA KVLGENEDVV RIMSIHKSKG LEFPVVIIAG TGKQFNFMDM
NKSILFHHDL GFGPDYINLE KRIYYPTIVK EIIKNKIKLE TLSEEMRILY VAMTRAKEKL
IITGVLKDVS KELNRYSKEL EFADEDISEY TIIKGKSYLD WIVPAVMREK DSNVLREKLE
DFNCAFNIID SKTKWYIKIW KSKDIIKKEE SEEQSLDVKE YLQSLDCSEN KSGYKEEIIK
RLNWKYKFNE SSNIPAKISV SELKRKFEEI EYENTLSMYD SKEDMNKSFL KKPIFLEKTK
KFTAAERGTL MHLVMQHIDL TKKLSKEEIK EQVSNMILKE FLTQEQSKVI NINQIYNFFN
SDLGKRMLNS KNIKREVPFY IEISSKDIYK NLPSIYENEK IMLQGVIDCY FEEKDYIVLL
DYKTDYVENI EHIKDKYSIQ LNYYKKALER ITGKSVKEMY IYLFFNDEII VY
//
