ID ADDA_HELMI Reviewed; 1396 AA.
AC B0TDI0;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=ATP-dependent helicase/nuclease subunit A {ECO:0000255|HAMAP-Rule:MF_01451};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01451};
DE EC=5.6.2.4 {ECO:0000255|HAMAP-Rule:MF_01451};
DE AltName: Full=ATP-dependent helicase/nuclease AddA {ECO:0000255|HAMAP-Rule:MF_01451};
DE AltName: Full=DNA 3'-5' helicase AddA {ECO:0000255|HAMAP-Rule:MF_01451};
GN Name=addA {ECO:0000255|HAMAP-Rule:MF_01451}; OrderedLocusNames=Helmi_28800;
GN ORFNames=HM1_2996;
OS Heliobacterium modesticaldum (strain ATCC 51547 / Ice1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Heliobacteriaceae;
OC Heliomicrobium.
OX NCBI_TaxID=498761;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51547 / Ice1;
RX PubMed=18441057; DOI=10.1128/jb.00299-08;
RA Sattley W.M., Madigan M.T., Swingley W.D., Cheung P.C., Clocksin K.M.,
RA Conrad A.L., Dejesa L.C., Honchak B.M., Jung D.O., Karbach L.E.,
RA Kurdoglu A., Lahiri S., Mastrian S.D., Page L.E., Taylor H.L., Wang Z.T.,
RA Raymond J., Chen M., Blankenship R.E., Touchman J.W.;
RT "The genome of Heliobacterium modesticaldum, a phototrophic representative
RT of the Firmicutes containing the simplest photosynthetic apparatus.";
RL J. Bacteriol. 190:4687-4696(2008).
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:0000255|HAMAP-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:0000255|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:0000255|HAMAP-Rule:MF_01451};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01451};
CC -!- SUBUNIT: Heterodimer of AddA and AddB/RexB. {ECO:0000255|HAMAP-
CC Rule:MF_01451}.
CC -!- SIMILARITY: Belongs to the helicase family. AddA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01451}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000930; ABZ85505.1; -; Genomic_DNA.
DR AlphaFoldDB; B0TDI0; -.
DR SMR; B0TDI0; -.
DR STRING; 498761.HM1_2996; -.
DR KEGG; hmo:HM1_2996; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000008550; Chromosome.
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 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; DNA damage; DNA repair; DNA-binding; Exonuclease; Helicase;
KW Hydrolase; Isomerase; Nuclease; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1396
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379274"
FT DOMAIN 26..532
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 615..920
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1171..1205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1190
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 47..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1396 AA; 156971 MW; 4E0C4CCEE9888B11 CRC64;
MNREALCHDD PIGHDRLRPD SIPRDPKWTD EQWQAITARN SDILVAAAAG AGKTAVLVER
LIGIIKEGVD VDRLLVVTFT NAAAAEMRER IRTALTKELA RHPHQTWLRQ QLVLLNRATI
TTLHSFCLDL VRKYYYRLDL DPAFRVADET EIALLRQDVL DEVFERFYER AGAKEGTESK
GEYFTALVDA YGGDRDDSPL QDIVLQLYEK ALSQPWPEQW LQDILGKFQE AGDTIAEQTL
PGELPAWEAL PWFAALREEM SIDLAEVESL LVRALSLCRQ PGGPAAYGDA VTADLQLTQD
LHLAAGRSWT QLHECFQALS FTRVKAVRGP VDESLKKEVS RLRYQAKKKL TDLQKKYFLR
TPHDLVSDLT QVLPLMATLV DVVLAFDRAF QAAKREKRLV DFNDLEHFCL RLLLDESASP
GVPVPSSLAL ELKEHFAEVL TDEYQDTNTV QETILTLLSR NNRFMVGDVK QSIYRFRLAE
PNLFLEKYRS FSPYDTPGPV NSDHGAPDHA FSGQGASVPG ARIDLAKNFR SRRNVLSAVN
DLFRRIMTPR AGEMAYDRQA ELVYGAAFPE LPGRSGDPVI ELWLLQRQPD ADGSEESIET
QQNANETKGA IDGDHKNIAK AGESPAQNTA DVAGESPSDD AGEDAGQPTG GEEELLLLET
AQYEARLAAR RIEELMKSAM PVYDREQGGY RPVCYRDIVI LMRSTKGRAD IFLEEFRAAA
IPAYADTGAG YFEATEVSIL LSLLRVIDNP CQDIPLAAVL RSPIFRFTGE DLARIRLAEP
RKTFFDAIEA FIGQAEAAAR DTFTPIDPVA IRLREFLRQI DAWRTLARRD SLAKLIATIY
RETGFYDYAG AMPGGGQRQA NLRALYDRAR QYEATTLRGL FRFLRFIERL QDQGGDLGTA
RTLGEKEDVV RIMSIHKSKG LEFPVVFVAG LGSQFNLQDL RRDLLIHKNL GLGPVVVDTQ
LRYRYPTVAK LAIQRRLHRE TLAEEMRILY VALTRAKEKL ILLGTVREVA KSAQQWLHDA
EGIPVAAALP DEVLLRAKCY LDWIGPALVG HPDGQEIRRW AEGAPALGAT LPENNLTMTK
NETMTEQERI DGSSRWRLFY AAKKELIGLR KETGSETPFN PVWLEKLRRL EPIIPTDLVD
ASLSWSYPYT GLSGIAAKVA VSRIKKQFVW HSPETPPSSE TPPSLEIPPS LETPPSLETQ
TPSPDALVDL RPRFLQQDRR LTATERGSAV HLFLQHLDLA GEISQAGIAG QADRLVKLEL
LSLEQRQALN EEEILRFLES PLGHRLRKAK QVMREVPFTL ALPAAEIYPE KRAEGESVII
QGVIDCLFEE DDGWLLLDYK TDRCPVGMDR ERWLQQLRDS YLGQVNLYHR AVESVLKVKV
KGRCLFLLSI GREMAL
//
