ADDA_STRU0
ID ADDA_STRU0 Reviewed; 1220 AA.
AC B9DRV0;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=SUB0686;
OS Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=218495;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-854 / 0140J;
RX PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A.,
RA Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R.,
RA Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D.,
RA Parkhill J.;
RT "Evidence for niche adaptation in the genome of the bovine pathogen
RT Streptococcus uberis.";
RL BMC Genomics 10:54-54(2009).
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; AM946015; CAR41583.1; -; Genomic_DNA.
DR RefSeq; WP_012658204.1; NC_012004.1.
DR AlphaFoldDB; B9DRV0; -.
DR SMR; B9DRV0; -.
DR STRING; 218495.SUB0686; -.
DR EnsemblBacteria; CAR41583; CAR41583; SUB0686.
DR KEGG; sub:SUB0686; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR OrthoDB; 137860at2; -.
DR Proteomes; UP000000449; 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: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; 2.
DR PANTHER; PTHR11070:SF48; PTHR11070:SF48; 2.
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; Reference proteome.
FT CHAIN 1..1220
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379357"
FT DOMAIN 26..482
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 519..807
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT REGION 533..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..557
FT /note="Basic and acidic 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 1220 AA; 140899 MW; D955BD07E39CCA45 CRC64;
MRFEPFLNQE EIRQLQEFEK NGSKAQKRTP EQIEAIYTNG QNILVSASAG SGKTFVMVER
IIDKVLRGIS IENMFISTFT VKAANELKER LEKKLREGIL MTDDPEMKAY LNDQMQAIAL
ADIGTMDAFT QKLLNEHGYL LGIPPKFRIM QDKSEQELLK NEIYKSLFEN YMASDHSQVF
LRLVKNFSGN RKDSKSFRDQ VYKIYQFSQS TENPKQWLEN NFLLAANQYQ DYDDLPDETI
DALLQSMKET AISLRDLTDL EEYGQMTKAG KPTAKYVKHL TMIEALNDWS MHFDSYYGKS
QIGKLAQDLS ALLPSGTDVT VAGQKYPIFK DIQSKISQFR HLATLLTYQP ETLPLLLELQ
SFVIDFTEAY LEAKKSENAF EFTDITHFAI EILQNEEAIR KVYQSKYHEV MVDEYQDNNH
MQECLLELLS NGHNRFMVGD IKQSIYRFRQ ADPQIFNQKF KDYQENPENG KLILLKENFR
SQSEVIDATN AVFSHLMDEA VGDILYDDNH YLKAGSDKQK IRYPENNCQV LIYDTDQKDN
GEDEHDKEDE RRTEGQETLS PGEVNILVKE IIRLHQEEAV PFSDITLLVS SRTRNDLLFK
TFNQYDIPLV SDGGQENYLK SVEVMVMLDT LRSINNPLND YALVALMRSP MFAFNEDQLA
RIALQDSQEG KVEHFYEKVL NSLSHQGQHA ELITQELHDQ LELFDQSLNA WRDYSRTHSL
YELIWKIYND RFYFDFVGLS PKAEQAQANL YALALRANQF EKTTFKGLTR FISMIDNILN
TENDLADVDL AKPKEAVNVM TIHKSKGLEF KYVFILNCDK KFSMADIHSP LILSRQKGVG
IKFLADVKKE LNATQLPSVK LYLETLPYQI NKKELKIATL SEQMRLLYVA MTRAEKKLYL
IGKGSQEKLS QKFDTKREGQ HLPKALRESI TNFQDWLLAI HQVFDSKDLS FTIDFVTDNE
LGPESIGSIS HQSNIMIDDL RDNRQSDSIA RAIDMLNNVN QLNQKYEAAI NLPTVRTPSQ
LKKFYQPIMD IDGVEILADK SQTPTTFELP QFSKAKQVTS SQVGSALHEL MQRIKITSHV
TEKDIQQASQ LVDAEAEVMA KIDLHKVKSF FEATELGRLI QVHHDKLYRE APFAMLKTDP
QSQEKFVIRG IVDGFLLLED KIILFDYKTD HYKTPLEMKL KYQEQMALYA ESLRKAYDIS
TIESYLILMG KERIEIVECS
