ID H3SDX6_9BACL Unreviewed; 1443 AA.
AC H3SDX6;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 66.
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=PDENDC454_08625 {ECO:0000313|EMBL:EHQ62652.1};
OS Paenibacillus dendritiformis C454.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1131935 {ECO:0000313|EMBL:EHQ62652.1, ECO:0000313|Proteomes:UP000003900};
RN [1] {ECO:0000313|EMBL:EHQ62652.1, ECO:0000313|Proteomes:UP000003900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C454 {ECO:0000313|EMBL:EHQ62652.1,
RC ECO:0000313|Proteomes:UP000003900};
RX PubMed=22461558; DOI=10.1128/JB.00158-12;
RA Sirota-Madi A., Olender T., Helman Y., Brainis I., Finkelshtein A.,
RA Roth D., Hagai E., Leshkowitz D., Brodsky L., Galatenko V., Nikolaev V.,
RA Gutnick D.L., Lancet D., Ben-Jacob E.;
RT "Genome Sequence of the Pattern-Forming Social Bacterium Paenibacillus
RT dendritiformis C454 Chiral Morphotype.";
RL J. Bacteriol. 194:2127-2128(2012).
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:EHQ62652.1}.
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DR EMBL; AHKH01000017; EHQ62652.1; -; Genomic_DNA.
DR RefSeq; WP_006676238.1; NZ_AHKH01000017.1.
DR STRING; 1131935.PDENDC454_08625; -.
DR PATRIC; fig|1131935.3.peg.1765; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000003900; 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; 6.10.250.2380; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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:UP000003900}.
FT DOMAIN 60..533
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 588..913
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1148..1213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 81..88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1443 AA; 161574 MW; 60E0E2E092D4F838 CRC64;
MDNNRDERNS REYESGSEAG GASRLPVAGE DGEGRVLTAA AASVGEAEAP AKLPPRPPES
TWTEEQWQAI VDGGENILVA AAAGSGKTAV LVERIISRIS DEAAMLHVDQ LLVATFTKAA
AAEMRERIRL ALERKLEANP DSEHLRRQLA LLNRASITTL HSFCLEVIQR HFQAVQLDPA
FRVANETEIE LLRQDVLEEL FEERYASKEP AFARMVDWFS GERNDEAAFR LVHRLYDFSR
SHPWPEEWLD SMTASFGPAD IAELGRSPWA DSIMAAARLT LNGIVELLRQ AIALTTAPGG
PEPYRAALEQ ELAGAAALAD AASSVPWERM HESFGLLSFG RLAACRGDQY DKELQEQVKR
LRDQAKKRLQ QVSDELFRRT PEQFLQELHA IRPVLETLAS VVREFGARFE AAKRAKGWLD
FADLEHYCLR ILRDPSSTPE RPVPSAAALQ YQEQFAEILL DEYQDTNMVQ EAIVDLITRP
GQGNRFMVGD VKQSIYRFRL AEPGLFQSKY TSYGKQGRGD GIRIDLARNF RSRQGIVDTV
NMVFRQIMNA DVAELTYDSA AELVCGASYP SAEEIAAESR RSRDEFGMPY FATELLLIDK
GVPAPADEAA EDEDGETERA AADAAELETA RLEARAIASR IRRMTGDEGE PPYLVYDKDQ
KRMRPVTYRD MVILLRATQA WAPLMLEELR REGIPAYAEF STGYFTATEV EIVLSLLRVI
DNPQQDIPLA AVLRSPIVGL QEEEMAQIRL YGKGKPFYYA VMEAARAEAE DGSPAAMQLE
LELPLSADEG ADMPPRQGRG SWQAKLIRFL DRLEQWRIAA RQGRLSELIW RVYRETGYYE
WVGGLAGGLQ RQANLRALYD RARQYESSSI RGLFRFLRFI DRMRDTGGDL GTARALGERE
DVVRIMTIHK SKGLEFPVVI VAGLSKRFNQ QDLNASFLMH KHLGFGPKYV DEEKRVAYPT
LPNLAIRRQM RLELLAEEQR VLYVALTRPK EKLILIGTVQ DAEKSIRKWG EALDVERLLL
PDYLVAEARS YLDWIGPAII RHPAAAEWRR YAGLPNRNGE CLLEDSSRWQ LAMVPASVIA
ADERLAEMPE DEERARRMKA LRKLETDDSF PRSAWADLIG ERLSWRDPHR IVTLLPSKTS
VTEMKRLAAT DDWPPEDWVG APAGAEGEAE ETAEKPGGLE AAETATGGNE PAAAAGAAAG
GDQAASGPYA DPSRTLYLRR PKFMERRGIT PVERGTAYHL LMQHLPLDRR LTAAEVNHTL
DALVARLIMT RLQADALDAE SVAAFFDSEV GRQLAEASWV KRELPFSYGL SATEAYTIEG
LRRRESVTAA AEALGSGTAS ASGNEPRFVA TPAFAAMDSS GQLDQEMVLV QGIIDCLFEW
NGELVLLDYK TDKVLAHRGG LRGLTEHYRF QLELYARAIE DIWKRPVKRK VLYFFDAKQA
CEL
//
