ID A0A1X7FHN1_9BACI Unreviewed; 1236 AA.
AC A0A1X7FHN1; A0A0H4KB20;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=B1B01_16755 {ECO:0000313|EMBL:OXS67145.1}, BEH_03580
GN {ECO:0000313|EMBL:AKO91272.1}, SAMN06296056_104133
GN {ECO:0000313|EMBL:SMF52332.1};
OS Priestia filamentosa.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=1402861 {ECO:0000313|EMBL:SMF52332.1, ECO:0000313|Proteomes:UP000192915};
RN [1] {ECO:0000313|EMBL:AKO91272.1, ECO:0000313|Proteomes:UP000036202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hbe603 {ECO:0000313|EMBL:AKO91272.1,
RC ECO:0000313|Proteomes:UP000036202};
RX PubMed=26248285;
RA Jia N., Du J., Ding M.Z., Gao F., Yuan Y.J.;
RT "Genome Sequence of Bacillus endophyticus and Analysis of Its Companion
RT Mechanism in the Ketogulonigenium vulgare-Bacillus Strain Consortium.";
RL PLoS ONE 10:E0135104-E0135104(2015).
RN [2] {ECO:0000313|Proteomes:UP000036202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hbe603 {ECO:0000313|Proteomes:UP000036202};
RA Jia N., Du J., Ding M.-Z., Gao F., Yuan Y.-J.;
RT "Genome Sequence of Bacillus endophyticus and Analysis of its Companion
RT Mechanism in the Ketogulonigenium vulgare-Bacillus strain Consortium.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AKO91272.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Hbe603 {ECO:0000313|EMBL:AKO91272.1};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Proteomes:UP000215399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27955 {ECO:0000313|Proteomes:UP000215399};
RA Dastager S.G., Neurgaonkar P.S., Dharne M.S.;
RT "Bacillus sp. V-88(T) DSM27956, whole genome shotgun sequencing project.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|Proteomes:UP000192915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGD-14 {ECO:0000313|Proteomes:UP000192915};
RA Varghese N., Submissions S.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:SMF52332.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27955 {ECO:0000313|EMBL:OXS67145.1}, and SGD-14
RC {ECO:0000313|EMBL:SMF52332.1};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-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}.
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DR EMBL; CP011974; AKO91272.1; -; Genomic_DNA.
DR EMBL; MWSI01000004; OXS67145.1; -; Genomic_DNA.
DR EMBL; FXAJ01000004; SMF52332.1; -; Genomic_DNA.
DR RefSeq; WP_040057172.1; NZ_MWSI01000004.1.
DR AlphaFoldDB; A0A1X7FHN1; -.
DR KEGG; beo:BEH_03580; -.
DR PATRIC; fig|135735.6.peg.670; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000036202; Chromosome.
DR Proteomes; UP000192915; Unassembled WGS sequence.
DR Proteomes; UP000215399; 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: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; 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:UP000036202}.
FT DOMAIN 11..484
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 511..805
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 1021..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1236 AA; 142894 MW; BA6133AE72AE389B CRC64;
MTDLREKPVN SQWTDDQWKA IVATGQDTLV AAAAGSGKTA VLVERIIGKL IDESSPIDVD
QLLVVTFTNA SAAEMKHRIG EALEKELKKA PSSLHLRRQL NLLNKASIST LHSFCLNVIR
NYYYKIDIDP GFRIADDTEA ELLRDEALQE LFEDYYSRED NLQFLDVVDR YTSDRSDAEI
QEIVRKMYEF SQSTPSPAMF LDELLLQYKV NENTRISDLS FMPFLMNEVR KQLHSVEDLL
NQGLALTKKP DGPAPRSVNF EEDLEQLQKI QSGAALSFEE AHEAMRNLTF SRLKPCKKGE
YDQNLVDQSS DIRKAAKEKL EKLHSELFSR PLTAYIDDML DMKPVIEVLT ELVKEFSKRY
SLKKREKGLV DFGDLEHYCL AILTEERDGE IERSAIAKQY ASQFHEVLVD EYQDTNMVQE
TIIKLVTRDE ESTGNLFMVG DVKQSIYRFR LAEPFLFLNK YKRFTKDGRT GGLRIDLNKN
FRSRSEVLDA TNYLFYQIMD EGVGEISYDS DAELKKGASY PSDENMATEL HLIEKNGADV
PVQEGEFSTE ELETSQLEAR LMAGKIKEMV QNRFQVYDAK KGITRNVTYR DFVILLRSMT
WAPQILEEFK EQGVPLYANL SKGYFEATEV TIMLSLLKVI DNPYQDIPLA SVLRSPLVRL
NDEELASIRL YDEKGTYYEA LKAYLKEASA EDEKYKDVEH FYHCLLKWRK EARQRPLYTL
IWNLYRETGF FEFVGGLPGG KQRQANLNAL YDRARQYEST SFRGLFRFLR FIERMQERGD
DLGTARALGE QEDVVRLMTI HSSKGLEFPI VFLAGIGRSF NLMDVNKSYL FHKELGFGSK
RINPRLRVAY PTLIQQAMKR KIRRESIAEE MRVLYVALTR AKEKLILVGT TSDKEKLVNK
WESVFYHEDV LLQSAVREEA KSYLEWIIPS LIRHRDFESF AHNQPASNQE LYNHPSKWEL
NVVPSFSLQE SEKKKEEEDK DLVEAIKNSQ QVKIQSPYRE EIERRLGWRY AYQQASKTKS
KQSVSELKRQ SQLLDEEEQT KGFQKPITER PLFLQAKKLT SAEKGTAMHT VMQHIPLKTD
VTEASLRELC SSLITREILT EKEASSININ GLLGFFDSEV GQRLQQAPSV YREMPFSFSA
KASELEQNWE GKEEPVLIQG IIDCLFRDEK GVVLLDFKTD DIANRFQGDF EKARDTLLSR
YKTQLNLYTR AVEEIGSIHI SERYLYFFDG GHFLSL
//
