ID   ADDA_BACP2              Reviewed;        1234 AA.
AC   A8FBR1;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=BPUM_0994;
OS   Bacillus pumilus (strain SAFR-032).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=315750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAFR-032;
RX   PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA   Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA   Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA   Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA   Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA   Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA   Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA   Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA   Weinstock G.M.;
RT   "Paradoxical DNA repair and peroxide resistance gene conservation in
RT   Bacillus pumilus SAFR-032.";
RL   PLoS ONE 2:E928-E928(2007).
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; CP000813; ABV61678.1; -; Genomic_DNA.
DR   RefSeq; WP_012009495.1; NZ_VEIS01000007.1.
DR   AlphaFoldDB; A8FBR1; -.
DR   SMR; A8FBR1; -.
DR   STRING; 315750.BPUM_0994; -.
DR   EnsemblBacteria; ABV61678; ABV61678; BPUM_0994.
DR   KEGG; bpu:BPUM_0994; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   OrthoDB; 137860at2; -.
DR   Proteomes; UP000001355; 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; 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; Reference proteome.
FT   CHAIN           1..1234
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379242"
FT   DOMAIN          9..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         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ   SEQUENCE   1234 AA;  142263 MW;  06DF5F0BC0F3E06F CRC64;
     MQIPKPNNST WTDDQWEAIV SEGQDILVAA AAGSGKTAVL VERLIRKMTR PEHPVDVDRL
     LVVTFTNASA AEMKHRITEA LEKELAKNPG SLHMRRQLSL MNRANISTLH SFCLQVLRTF
     YYEIDLDPGF RLADQTEGEL LGDEVLDELF EDEYKAGKPS FFELVDRYTS DRHDLDLQWL
     VKRIYDFSRS HPSPEQWMRA FLSLYDVDAQ TKVEELPFYP YIKEDLSLVL RSCQELLERA
     LSLSKEPGGP APRAENFIDD LEQVNELIRH QDDFEKLYEL LPNVNFKRLK TCKGDEYDPV
     LLEKATDARN QAKKQLEKLK DEYFMRSPAQ HLKSLAEMKP IVETLVELVI QFGERFERAK
     QEKSIVDFSD LEHYCLRILA EQDAEGHLIE TEAAKYYQQQ FEEVLVDEYQ DTNLVQETIL
     KLVSKGEHSS EGNLFMVGDV KQSIYRFRLA EPMLFLNKYK HFQPDGKETG KRIDLNKNFR
     SRSDVLDSTN FLFKQLMGET VGEIEYDEQA ELKLGASYPE SKDTTTEMLL VHLDQQEAET
     GEEREELETV QFEARIIAKK IKELVEQPFQ VYDAKQQMTR NLQYRDIVIL LRSMPWAPQM
     MEELKKQGIP VYANLSSGYF EATEVSVILS LLKVIDNPYQ DIPLAAVLRS PLVHLDENEL
     ALIRTSDKKG TYYDAVKAFM SVTHSDHPTC KKLERFFQLL RKWRDFSINH SVAELIWEVY
     RDTQYLDYVG GMPGGKQRQA NLRALYDRAK QYEKAAFRGL FRFLRFIERM QERGDDLGAA
     KTFSETEDVV RMMTIHSSKG LEFPVVFTVG LGRNFNMMDL NQSYLLDKEL GFGSKYIHPE
     LRISYATLPL VAMKKKMRKE LLSEELRVLY VALTRAKEKL FLVGSVKNQV KALSKWQNAA
     TGEEWLLPDF ERYQSKTYLD FIGPALIRHQ AMSSVLEETG DVVLSHPSTF TISFTQASDL
     LKEDMSLEKK EQDEIVQALM DGLPVEGYGD ADEKVAERLS WKYPYLAASQ VGTKQSVSEI
     KRMKEIQDEY SVPSSIRKAR ATLYDRPAFM KKKTLTAAEQ GTAMHTVMQH IPLPSEEPYD
     ESRIGHLLDS LQQRDLLTDE QVQSINQEGI AAFFSTSIGQ KLLKADWVKR EVSFSMVLPV
     KEVYSHIDTE GEPVLIQGMI DCLFETDGKL YLLDYKTDRV QGRYTGGIDA AVPILKKRYE
     TQIALYAKAV ERLTNRTLEE KILYFFDGNV EISL