ID A0A0F2NK90_9FIRM Unreviewed; 1255 AA.
AC A0A0F2NK90;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=VR68_04800 {ECO:0000313|EMBL:KJS01591.1};
OS Peptococcaceae bacterium BRH_c4a.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=1629716 {ECO:0000313|EMBL:KJS01591.1, ECO:0000313|Proteomes:UP000033439};
RN [1] {ECO:0000313|EMBL:KJS01591.1, ECO:0000313|Proteomes:UP000033439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c4a {ECO:0000313|EMBL:KJS01591.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-2015) 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:KJS01591.1}.
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DR EMBL; LADN01000033; KJS01591.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2NK90; -.
DR STRING; 1629716.VR68_04800; -.
DR PATRIC; fig|1629716.3.peg.1607; -.
DR Proteomes; UP000033439; 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; 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|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}.
FT DOMAIN 5..482
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 535..826
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 26..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1255 AA; 141874 MW; A5CA1556784D9EC6 CRC64;
MKENTNWTGE QWEAITGKDC NLLVAAAAGA GKTAVLVERI IRKITDPGNP VDIDRLLIVT
FTNAAATEMR ERIAEAISAV LEKNPGSKNI QRQLTLLNKA SITTIHSFCL EVIRSNFQSI
NIDPGFRITD ETEAALMKLE VLNDLFEDQY EKEENGDFFE LLECYGGNRD DQAVQDMVLN
LFSFIQSSPW PEKWLDGMTE SFNAPEGLDF GDTPWGRVLL NSVMLELCGL KEMIARAADI
LKYAAGLEKY LNVYLEDLSS LDALSKVCTD ESGTKWDAVY GAIQSLEFKR LPSAGKDADK
EKQEYVKKIR DDVKARIKRM KEKTFTADSA EILNDMKAMY PIMKCLAGLV SDFGERYSAK
KSQKSVVDFN DLEHFCLEIL SQKDEHGEIS PSGAALGYRD RYAEILVDEY QDSNLIQEIM
ISMVSRADTA KPNVFMVGDV KQSIYRFRQA KPELFLDKYS SYSTEKGNPF RKILLFKNFR
SRKEIVNAVN FIFQQIMSVS VGELDYTDIE ALNPGAVFAE NDKETTVAGG AAEFHLIQTG
GGGNIISEEE LSGEEQESAE EEPDDEEMLD SIQCEARLAA KRIRELMQPD DQGREFRIFD
RGRKAYRKAD YRDMVILLRT VRRWSDVFME ELAMRGIPAF ADTGAGFFKT SEVQVILSLL
QIIDNPLQDI PLLSVIRSPI VSFTTDELAE LRLARRKAAL YDALQVLAQG GESQAAKKAA
SFLNDLRRWR DMSLYMATDQ LLWQLYNETG YFGTVGAMPA GEQRQANLRI LFERARQFEE
TAYKGLFNFI NFVDKLKSSK GDMGSAKILG ENDNVVRIMS IHKSKGLEFP VVILSGCGKK
FNLQDMNKSI LLHQELGFGP DVVDHRRRLS YPSAPKQAIR EKIKAETLSE EMRILYVALT
RAREKLIITG AVRDVPKAAA KWAKCADVPE HKLPAYEMLK GGSYLDWIVP ALLRHKDCGV
FRESAGIGSR FGGLLIEDPS VWGIRIWNKS DVLSGKTAKE HDQSQFIQWL DGLDTAEQAD
AFPEEIAGRL SWEYQYEKAS KVPAKVSVTE LKRRFDAELL GETGAFSGYL PALVKKPLFL
EEKKGLSAAE AGTVLHFVMQ RLNYKQVDME AQIEEMVAKD LLTEQQAKSV DVDKIRRFLE
SPLGSRLLAS ESVNREVPFN MEIPCHELYP DMRGEAYQGE TLLLQGVIDC YFEEPDGIVL
LDYKTDYAPV GKVETIRERY RLQISYYARA LEMLTGKKVR EKYIYLFWNG EVLVI
//
