ID ADDA_STRMU Reviewed; 1212 AA.
AC Q8DT76;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 124.
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}; Synonyms=rexA;
GN OrderedLocusNames=SMU_1499;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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}.
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DR EMBL; AE014133; AAN59152.1; -; Genomic_DNA.
DR PIR; A43258; A43258.
DR RefSeq; NP_721846.1; NC_004350.2.
DR RefSeq; WP_002262919.1; NC_004350.2.
DR AlphaFoldDB; Q8DT76; -.
DR SMR; Q8DT76; -.
DR STRING; 210007.SMU_1499; -.
DR DNASU; 1028745; -.
DR KEGG; smu:SMU_1499; -.
DR PATRIC; fig|210007.7.peg.1334; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OrthoDB; 9810135at2; -.
DR PhylomeDB; Q8DT76; -.
DR Proteomes; UP000002512; 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 CDD; cd17932; DEXQc_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; DNA damage; DNA repair; DNA-binding; Exonuclease; Helicase;
KW Hydrolase; Isomerase; Nuclease; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1212
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379332"
FT DOMAIN 26..482
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 510..800
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT BINDING 47..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1212 AA; 139292 MW; 1387B78FF975D187 CRC64;
MTFKPFLTDQ EIASLQIQEA QSDKKQKRTP EQIEAIYTSG TNILVSASAG SGKTFVMIER
IMDKILRGVT IDQLFISTFT VKAAGELKER LEKKITEQLR LTNDTALKQF LSEQLLGLQT
ADIGTMDAFT QKLVTQYGYT LGISPNFRIL QDKSEQDLLK NDVFDDLFTD YRTGDQAELF
TKLVRNFAGN RKDSSNFRQI IYKIYDFSQA TDNPQRWLLE NFLKGANTYK DFSAIPEQEV
KDFLNTLQET ALALRDVTDL EDYKQVTAKG TPTAAYQRHL KMIEQLQDWV LHFDSLYGRD
GLGKLANDIA TLIPSGNDVT VAGVKYPVFR SLHSRLRGLK HLETIFKYQD QSLPLLQVLQ
SFTLDFSKQY LQAKMQENAF EFSDIAHFAI QILEENDAIR QLYIDKYHEV MVDEYQDNNH
TQERMLELLS NGRNRFMVGD IKQSIYRFRQ ADPQIFNQKF KDFQEHPEHG KLILLKENFR
SQSEVLDATN SVFTHLMDEA VGEILYDDTH QLVAGSSAQK IPYPQNETQV LIYDTKDQQN
QDLAVEDDSN QISLGEVKLV AKEIIRLHNE EKVQFEDITL LVSSRTRNDG ILQTFDDYGI
PLVTDGGEQN YLKSVEVMVM LDTLRSIDNP LNDYALVALL RSPMFAFDED DLARLALQNL
PDQHKQNLYE KMENARNGQG QQVQLITEAL SAKLDAFFET FLSWREFSLL NSLYDLIWKI
YNDKFYYDYV GSLPKSEQRQ ANLYALALRA DNFEKTGFKG LSRFIRMIDK ILENQNDLAD
VEVALPKNAV TLMTIHKSKG LEFKYVFILN IDKKFSIQDM TSPLILSRQN GVGIKYIADM
KEELEEKLLP TVKVSMDTLP YQLNKRELRL ATLSEQMRLL YVAMTRSEKK LYLVGKGSQE
KLGDQYDGKS ENNHLPVADR EHYLTFQDWL LAIEAAYAAD ELHFKTSFIT DEDLTEDKMG
SLEAEQAYDA DNLKDNRQSD DITRALDMLE AVEKLNQHYK AAIHLPTVRT PSQIKKFYEP
VMETEGVEVM QTSYQTKPKF ELPQFSKKAK QDPTALGSSV HELMQRLHLS EQVSLEDILT
ALAELSVEEN VKKAIQVDKI LHFFQTSQLG KLIQANADKV YREAPFAMLQ ADPASGEDYV
VRGIIDGYIL FDNRIVLFDY KTDKFTNSQA IKERYRGQMT LYAQALSQSY NIQQVDSYLI
LLGGEKLEVV EI
//
