ID A0A1G7Z8E1_9BACI Unreviewed; 1223 AA.
AC A0A1G7Z8E1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=SAMN05192534_101440 {ECO:0000313|EMBL:SDH04867.1};
OS Alteribacillus persepolensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alteribacillus.
OX NCBI_TaxID=568899 {ECO:0000313|EMBL:SDH04867.1, ECO:0000313|Proteomes:UP000199163};
RN [1] {ECO:0000313|EMBL:SDH04867.1, ECO:0000313|Proteomes:UP000199163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21632 {ECO:0000313|EMBL:SDH04867.1,
RC ECO:0000313|Proteomes:UP000199163};
RA de Groot N.N.;
RL Submitted (OCT-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; FNDK01000001; SDH04867.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7Z8E1; -.
DR STRING; 568899.SAMN05192534_101440; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000199163; 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; 2.
DR CDD; cd18807; SF1_C_UvrD; 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};
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:UP000199163}.
FT DOMAIN 12..474
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 501..796
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1223 AA; 141036 MW; D354CA2905DED086 CRC64;
MKLKWKQKPE GAFWTDSQWE AVSGSGSNQL VSAAAGSGKT AVLVERIIHK ITDQEHPVDM
DRLLIVTFTN AAAAEMKNRI AEALEAAINE KPGSLYLRRQ LALLNKAQIS TLHAFCMSLV
RKYYYKLNID PKFRIIDDIE GELLREEILD GVFESQYSKE NNEAFLDASE RFSGDKSDEG
FKQVVREVYR FSQAHPDPEK WLQDMAACYE VTGVSQMEDT PWGKEVLENV KTRLSASIDM
LQQAISLCQE EGGPLAYEET LLGDKQMLEE LYQATNWDTL YTRFQDVVFK RLKTVKKSED
IDETLKTRVK DMRDAVKKDV TDMKTETFTA SPADLLRDIK EMAEPVHALV STVSLFSNRY
QLAKTEKGVV DFSDLEHFTL RILQEEGSEA AEQYRSRFDE VLVDEYQDTN LIQEAILRHI
SKGDNLFLVG DVKQSIYRFR LAEPSLFLDK YKQYNRTDGQ PGWKVNLDQN FRSRQEVLQA
SNFIFKQLMD EKVGDIVYDE TAELKTGNTD YPDNDEALPE LTLINKGDPI NTSIPDEEQE
DSDTASLEAR WIARKIKNMI KDGYQVLDKE TKAVRKMTYR DVVILMRSMP WAAVMMDEFK
KEGLPVYAEV SGGYFQAVEI NIMLSLLQVI DNPRQDIALA AVLRSPIVGM DEEELAKLRL
CDPKGMFFDA LKQAAHAVST NHEAWQEKAQ AFYEKLCRWR ERARNEALPK FIWDLFQETG
YYDFVGGLPG GKQRQANLTA LYDRARTYEK TSFRGLFRFL RFIERMQERG DDFGTARALG
EQEDVVRIMT IHKSKGLEFP VVFIAGMNKS FNLQDTYRSV LLHKELGIGA KTIDPIKRVM
KSSVAQQAVK HRIHRESLSE EMRVLYVAMT RAKEKLCLVG TVKNPEKTLA KWAQYKDVED
WLLPERDRVK AASYADWIGP AIFRHQSADS WYDTMHPSAC ADVYHYPVNW RITLVEQRDI
KEITEADELE NNETMTALKE RKPVLQESVY KHAVEEKLNW SYPYQAAVTE RSKKTVSEFK
RAFHDEYSEP VFQPEFHAQY AERPLFMQEK NTRPEEKGTA VHTVMEHLPL NMETVEDCQM
FIDTLVGREL LTEDQKNMVD AENIMMFLSS ALGKRLTSAA QVFREIPFSY GMQTDDGDTV
LIQGAVDCVF RDKEGQLVLI DYKTDAFQSR YPGNRERAEY AMREKYQSQL DVYRQALSAI
WQEEVAEAYL YIFDGHCVID MMK
//
