ADDA_LISMH
ID ADDA_LISMH Reviewed; 1235 AA.
AC B8DF44;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01451};
DE AltName: Full=ATP-dependent helicase/nuclease AddA {ECO:0000255|HAMAP-Rule:MF_01451};
GN Name=addA {ECO:0000255|HAMAP-Rule:MF_01451}; OrderedLocusNames=LMHCC_0276;
OS Listeria monocytogenes serotype 4a (strain HCC23).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=552536;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HCC23;
RX PubMed=21602330; DOI=10.1128/jb.05236-11;
RA Steele C.L., Donaldson J.R., Paul D., Banes M.M., Arick T., Bridges S.M.,
RA Lawrence M.L.;
RT "Genome sequence of lineage III Listeria monocytogenes strain HCC23.";
RL J. Bacteriol. 193:3679-3680(2011).
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=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=3.6.4.12;
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; CP001175; ACK38636.1; -; Genomic_DNA.
DR RefSeq; WP_012580845.1; NC_011660.1.
DR AlphaFoldDB; B8DF44; -.
DR SMR; B8DF44; -.
DR KEGG; lmh:LMHCC_0276; -.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
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:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 4.
DR Gene3D; 3.90.320.10; -; 1.
DR HAMAP; MF_01451; AddA; 1.
DR InterPro; IPR014152; DNA_helicase_suAddA.
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; PTHR11070; 1.
DR PANTHER; PTHR11070:SF48; PTHR11070:SF48; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
DR TIGRFAMs; TIGR02785; addA_Gpos; 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; Nuclease; Nucleotide-binding.
FT CHAIN 1..1235
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379297"
FT DOMAIN 12..482
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 509..800
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1235 AA; 142537 MW; 41013B3B5171D206 CRC64;
MSLNIPPKPE ESLWTDDQWK AIQAKGNNVL VAAAAGSGKT AVLVTRIIKK LIDESANLNV
DELLIVTFTN ASAAEMKFRI GKGLEEALGQ NPDSAHLKRQ VALLNYASIS TLHSFCLEII
RKYYFEADID PSFRLIEPIE SSMIRDEVLE GLLEQEYGIE NNEAFFHLVE SFTGDRSDAE
LHSLISKLYD FSRANPDPNA WLEAMVNFYN TEEITSITEL PYFPIIKEDI ELRVNQAKNY
LLNAIDYANE NNGPAPYLAT LENDLVQIQA LSELNWSSWT HLKTSIENID FKRIPTLKNK
SDYDEVYVEE AKKFRDAAKK EMKNIATDWF SREEVNYLSD LEKMKPDIQT LSELVKKFAA
NFFEEKQQRG VLDFNDLEHL ALKILLNGDK ASEVAQNYQK QFKEVLIDEY QDTNMVQETI
LRLVTNPSEA QGNLFMVGDV KQSIYRFRLA EPTLFMTKYQ TFQQDGSGNG IRIDLSQNFR
SRKEVLDATN FIFRQLMDKH IAEIDYDTAA ELTLGAKSPE TNAMATELLL IDMKTEDTET
EDELSPQELQ KNQVESRTIA MKIREMIDNK FPIYDKKLKQ NRPIQYRDIV ILSRAMTSAP
DMEEAMKVQD IPFYANNNSG YFETTEVATM IALMKVVDNP YQDIPLAAVL RSPIIGLNEE
ELGQIRMAKK KGYFYDALLA YKDITVSETA DKISDFVQQL NNWRELSIRE NLTSLIWQIY
QETNFYEFVG GLPGGKQRQA NLRALYDRAN QYEKTSFRGL FRFVRFVERL EIRGDDLGTA
KTLGEKEDVV RMMTIHASKG LEFPVVIVSG LSRKFNMRDI YSKTLLDKDY GFASSYRDVE
KMIVYPTIMQ QAIKQKKSRE MIAEEMRVLY VALTRAEEKL ILVATVPDFE KTSKNWLQVA
KEKETILPAA TRAKAKCYLD WIGNATIRHS AFKELLCEEM IQTLATEMKL QIEIKTKEMF
LTNELERAES DNWLENIKEH QPVPIQSPYK DEIQRYMEYE YQNEAATEIR AKQSVTELKR
QFSLQDNWSD TTLLKEFQKV SLDRPKFLQK NKLSATEIGT AMHTLMQAVS LDYKPTKEDL
EQLLRTMREK DILTDAQIKA INIKQILDFF ESPLGETMLQ KKDLVKREVP FSYLLPVSEL
YENVDIDERV LIQGVVDSMI EEEETITLID YKTDKIEGRY ADWNAAEKVM KERYHIQIKL
YAEAIQAISG KKVAAAYLYF FDGQHICQIN TKEGL
