ADDA_LACLS
ID ADDA_LACLS Reviewed; 1203 AA.
AC Q033I1;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=LACR_0004;
OS Lactococcus lactis subsp. cremoris (strain SK11).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=272622;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK11;
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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; CP000425; ABJ71641.1; -; Genomic_DNA.
DR RefSeq; WP_011675081.1; NC_008527.1.
DR AlphaFoldDB; Q033I1; -.
DR SMR; Q033I1; -.
DR PRIDE; Q033I1; -.
DR EnsemblBacteria; ABJ71641; ABJ71641; LACR_0004.
DR KEGG; llc:LACR_0004; -.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000000240; 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; 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; 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..1203
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379291"
FT DOMAIN 4..472
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 503..785
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1203 AA; 139010 MW; 3EC5E8341551A129 CRC64;
MSEVKLTPEQ NEAIHSSGKN ILVSASAGSG KTFVMAQRIV EKVKQGIEID RLFISTFTKK
AASELRMRLE RDLKKARQES SDDEEAHRLT LALHNLSNAD IGTMDSFTQK LTKANFNRVN
IDPNFRILAD QTESDLIRQE VFEQLVESYL SADESLNISK DKFEKLIKNF SKDRNILGFQ
KVVYTIYRFA SATENPISWL ENQFLKGFET YKSLTDLSED FTVNVKENLL TFFELLENSL
TNGVIAKKGA GRDKANLILD NKNELLEAIS KKDFVTFTAL FLSIDTDIRV GSSKDETLSA
LKKDFSAQKQ DLVGSKSKPG ELRKFVDKIK HGQLIEKYQK QAFEIASDLQ KFIIEFYKTY
LERKKNENAF EYSDIAHFAI EILEENPDIR ENLREHYDEI MIDEYQDTSH TQERMLELLS
NGHNLFMVGD IKQSIYGFRL ADPGLFLEKY KSYDQAENPN QLIRLKENFR SRGEVLNFTN
DIFKHLMDEK LGEMTYGKEK ALVQGNISDY PVEAEKDFYP ELLLYKENTS EEEIEDSEVK
ISDGEIKGAA QEIKKLIESG VEPKDIAILV RSKSNNNKIE DILLSYDIPV ILDEGRVDFL
KSMEVLIMLD ILRAIDNPLY DLSLVAMLRS PLFGFNEDEL TRISVQGSRD LRFWDKILLS
LKKEGKNPEL INLSLEQKLK AFNQKFTEWR KLVNQIPIHR LLWKIYTETY YFDYVGALKN
GEMRQANLQA LSVRAESYES SGYKGLFKFV RLINKFMEQN NDLASVNIKL PQNAVRVMTF
HKSKGLEFDY VFLMNLQSRF NDRDLKEDVI LSREHGLGMK YIADLKAEPD VITDFPYALV
KMETFPYMVN KDLKQRAALS EEMRVLYVAF TRAKKKLYLV GKIKDTDKKA GLELYDTATL
EGKILSDKFR NSSRGFQHWI LALQNATKLP MKLNVYTKDE LETEKLEFTS QPDFKKLVEE
SEKFDNIMSF SDEIKEAQKI MNYQYPHQAA TELSSIQTPS QVKKRSYEKQ LQVGEVQPVS
EFVRVKNLDF SDFGSKKITA AEIGSATHSF MQYADFSQAD LFSFQATLDE MGFDEKIKNQ
IDITKILTLF DTEFGKFLSE NVDKTVKEAP FSMLRTDEFA KEQYIVRGIC DGFVKIADKI
ILFDYKTDRF TNVSAISEIK ERYKDQMNLY SEALQKAYHV NQIDKYLILL GGPRKVFVEK
LDD
