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