ID A0A398B9N1_9BACI Unreviewed; 1252 AA.
AC A0A398B9N1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-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:RID86191.1};
GN ORFNames=D1953_10485 {ECO:0000313|EMBL:RID86191.1};
OS Peribacillus asahii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX NCBI_TaxID=228899 {ECO:0000313|EMBL:RID86191.1, ECO:0000313|Proteomes:UP000266016};
RN [1] {ECO:0000313|EMBL:RID86191.1, ECO:0000313|Proteomes:UP000266016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MA001 {ECO:0000313|EMBL:RID86191.1,
RC ECO:0000313|Proteomes:UP000266016};
RA Seuylemezian A., Vaishampayan P.;
RT "Bacillus jemisoniae sp. nov., Bacillus chryseoplanitiae sp. nov., Bacillus
RT resnikiae sp. nov., and Bacillus frankliniae sp. nov., isolated from Viking
RT spacecraft and associated surfaces.";
RL Submitted (AUG-2018) 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:RID86191.1}.
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DR EMBL; QWVS01000016; RID86191.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A398B9N1; -.
DR Proteomes; UP000266016; 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 CDD; cd18807; SF1_C_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; 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|ARBA:ARBA00023235, 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:UP000266016}.
FT DOMAIN 13..487
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 522..815
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT COILED 547..581
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1252 AA; 144372 MW; 07185CF6A0BE8E36 CRC64;
MSKTIIPEKP VDVTWTDDQW KAIWAKDQDI LVAAAAGSGK TAVLVNRIIQ KILSEDDPVD
VDELLVVTFT NASAAEMRHR ISEALEQAIA QNPSSQHLRK QLSLINRASI STLHSFCLEV
IRQYYYEIDI DPGFRIADST EIELLRDEVM EELFEEHYGR SDNEEFFRLV DAFTSDRSDA
DLQQIVRSLH DFSRSHPNPS QWLDEAAEMY DLSDDARIED LPFIQALRFD ISLQLDKAKD
LVEKALDLTK VPGGPAPRVE NYRADLEMIA VLSQANETSW YTLHEAIQNI SFTTAKRCSG
ADFIKEIVDE ATKHRDKAKK IVKTLQEELF VRKPESYLRD IRELKSYVET LVLLVKQFDT
RFFAAKTEKN LVDFSDLEHF CLEILTKELE HGERKPSDVA LAYRKQFKEV LVDEYQDVNL
VQESILSLVT ADGEHSGNMF MVGDVKQSIY RFRLAEPNLF LGKYNRFTHD GQESGLRIDL
NQNFRSRMEV LDGTNFLFQQ LMGIKVGEIE YDEDAQLKKG APYPEDQSFP IELYIVDGAP
NEEESLADSS ESTAEFESEE LEKAQLEARM MAKLIKQAIN EKQPIYDPKT KQYRAIQYRD
IVILLRSMPW APQIMEEFKK QGIPVYANLS TGYFEATEVA IMLSLLKVID NPQQDIPLAS
VLRSPIVGLD EEQMAKIRTF HSGSYYEALA AFYRQGDVNE QTGLYEQVAA FYRKLVKWRK
LAKQESLSDL IWLLYRETRF YDFVGGMPGG KQRQANLRAF YDRARQYESS SFRGLFRFLR
FIERMQERGD DLGAARALGE QEDVVRLMTI HSSKGLEFPV VFIAGLSKQF NMMDLRKSYL
LDKEFGFAAK YVNPELRITY PSLPQLAFKK KKQLELIAEE MRVLYVALTR AKEKLYLIAS
VNNAEKSLNS WWSNASHADW LLKDYTRAGA KSYLDWIGPA LIRHQDGQRL MEDHVPNRLN
ENITSHASQW MISIVRSEEL MGMDEEELAE DSWLEQVKQS KKVDSTSEYT SLIEDNLHWS
YPQINAATHR SKQSVSELKR RFELADDHSA TELIESFSRP ITKRSAFMQE KSLTPAEKGT
IVHLVMQHLD VTADITVDYI EQLLTNLIQR ELLTEEQRVA VDSHIIIQFF QTEIGQRLKK
AAIVRREVPF MMSLPAHIAY PDWDEGEEEV LVQGVIDCLF EDEQGLVLLD YKTDAITGRF
SNGFEGAKDI LAERYRTQLQ LYKRAVEGIL HKKVTKCYLF FFDGAHLLEM ER
//
