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ADDA_BACLD
ID   ADDA_BACLD              Reviewed;        1230 AA.
AC   Q65LJ9; Q62WZ0;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 120.
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};
GN   OrderedLocusNames=BLi01157, BL01350;
OS   Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS   NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=279010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC   / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15383718; DOI=10.1159/000079829;
RA   Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA   Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT   "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT   with great industrial potential.";
RL   J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC   / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA   Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA   Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA   Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA   Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT   "Complete genome sequence of the industrial bacterium Bacillus
RT   licheniformis and comparisons with closely related Bacillus species.";
RL   Genome Biol. 5:R77.1-R77.12(2004).
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; CP000002; AAU22718.1; -; Genomic_DNA.
DR   EMBL; AE017333; AAU40065.1; -; Genomic_DNA.
DR   RefSeq; WP_011197743.1; NC_006322.1.
DR   AlphaFoldDB; Q65LJ9; -.
DR   SMR; Q65LJ9; -.
DR   STRING; 279010.BL01350; -.
DR   PRIDE; Q65LJ9; -.
DR   EnsemblBacteria; AAU22718; AAU22718; BL01350.
DR   KEGG; bld:BLi01157; -.
DR   KEGG; bli:BL01350; -.
DR   PATRIC; fig|279010.13.peg.1140; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   OrthoDB; 137860at2; -.
DR   BioCyc; BLIC279010:BLI_RS05745-MON; -.
DR   Proteomes; UP000000606; 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..1230
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379241"
FT   DOMAIN          9..480
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          507..796
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   1230 AA;  141091 MW;  10DDC24F1AC42C2F CRC64;
     MEISKPKGST WTDDQWKAIV SSGRDILVAA AAGSGKTAVL VERIIRKITD QERPVDVDRL
     LVVTFTNASA AEMKHRIGEA LEKELAENPG SLHLRRQLAL LNKASISTLH SFCLQVIRKY
     YYLIDVDPAF RIADQTEGEL LGDEVLDELF EEEYKKGNPA FFELVDRYTT DRHDLDLQHL
     VKRVYEFSRS HPDPEGWLHS LAELYDAASD TKVEALPFYS YIKEDIALVL EGMRQKLTRA
     LDLTKQPGGP APRAENFLDD LAQIDRLIQQ QDDFSALHEL VPTVSFQRLK PCKGDEYDPR
     LVDEAADLRN SAKKQLEKLK SDYFSRTPEQ HLESLREMKP VIQTLVQLVL EYGRRFAEAK
     KEKAIVDFSD LEHDCLAILS VKNPAGEAVP SEAAKFYRHQ FHEVLVDEYQ DTNLVQEAIL
     KLVAKEEHEG NLFMVGDVKQ SIYRFRLAEP LLFLSKYKRF TDDGSGSGQK IDLNKNFRSR
     SDILDSTNFL FKQLMGEKVG EVEYDEQAEL KLGASYPPNE ATKTELLLIE TPSGAPGEEA
     EELEAVQLEA RAMAGQIRRL ITEKFQVYDA KAKASRNIQY RDIVVLLRSM PWAPQIMDEF
     KQQGIPVYAN LSTGYFEATE VSVTLSLLKI IDNAYQDIPL ASVLRSPVVG LDENELSLIR
     IKDKKAPFYE AMKAYLAAAD GDERLSEKLR RFDGLLKKWR AYAKNHSVAE LIWEIYRDTK
     YLDYVGGMPG GKQRQANLRA LYDRARSYEA TSFRGLFRFL RFIERMQERG DDLGTARALS
     EQEDVVRLMT IHSSKGLEFP VVFTAGLGRN FNMMDLNKSY LLDKELGFGT KFIHPKWRIS
     YPTLPLIAMK KKLRRELLSE ELRVLYVALT RAKEKLYLVG TAKDKEKLLA DWRTQAAGSE
     WLLPDYERFQ AKSYLDFIGP ALMRHRDMDE SGAPPVIDEI REHPARFQVS WLSAADLQAE
     AVDQAGEERH DRLVQIQMGH AIEGAFEYEQ QVRERLAWSY PYKDAAKVRT KQSVSEMKRQ
     KEYEDEYGDR SLIRPSQEAL LFKRPSFMMA KGLTAAERGT AMHTVMQHIP LTRTPEKNEL
     SRLLDRLVEK ELLTEDQRAA IEEDDILAFF DTEIGQKLFG ARRVEREVPF NMTLSAKEVY
     PDLESADEPV LIQGIIDCLF ETEDGFYLLD YKTDRIHGKY RNGFEGAEPI LRKRYETQIQ
     LYARAVETMI KMPLKGRALY FFDGGHVLLF
 
 
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