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Database: UniProt
Entry: Q033I1
LinkDB: Q033I1
Original site: Q033I1 
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   05-DEC-2018, entry version 86.
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=LACR_0004;
OS   Lactococcus lactis subsp. cremoris (strain SK11).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
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.,
RA   Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N.,
RA   Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K.,
RA   Goodstein D.M., Hawkins T., Plengvidhya V., Welker D., Hughes J.,
RA   Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B.,
RA   Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E.,
RA   Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C.,
RA   Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J.,
RA   Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S.,
RA   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
CC       helicase and an ATP-dependent, dual-direction single-stranded
CC       exonuclease. Recognizes the chi site generating a DNA molecule
CC       suitable for the initiation of homologous recombination. The AddA
CC       nuclease domain is required for chi fragment generation; this
CC       subunit has the helicase and 3' -> 5' nuclease activities.
CC       {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}.
DR   EMBL; CP000425; ABJ71641.1; -; Genomic_DNA.
DR   RefSeq; WP_011675081.1; NC_008527.1.
DR   ProteinModelPortal; Q033I1; -.
DR   SMR; Q033I1; -.
DR   EnsemblBacteria; ABJ71641; ABJ71641; LACR_0004.
DR   KEGG; llc:LACR_0004; -.
DR   HOGENOM; HOG000285114; -.
DR   KO; K16898; -.
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:0004003; F:ATP-dependent 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; 1.10.10.160; -; 1.
DR   Gene3D; 3.90.320.10; -; 1.
DR   HAMAP; MF_01451; AddA; 1.
DR   InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR   InterPro; IPR014152; DNA_helicase_suAddA.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR011604; Exonuc_phg/RecB_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038726; PDDEXK_AddAB-type.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   InterPro; IPR034739; UvrD/AddA_N.
DR   PANTHER; PTHR11070; PTHR11070; 1.
DR   PANTHER; PTHR11070:SF14; PTHR11070:SF14; 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; Complete proteome; DNA damage; DNA repair; DNA-binding;
KW   Exonuclease; Helicase; Hydrolase; Nuclease; Nucleotide-binding.
FT   CHAIN         1   1203       ATP-dependent helicase/nuclease subunit
FT                                A.
FT                                /FTId=PRO_0000379291.
FT   DOMAIN        4    472       UvrD-like helicase ATP-binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01451}.
FT   DOMAIN      503    785       UvrD-like helicase C-terminal.
FT                                {ECO:0000255|HAMAP-Rule:MF_01451}.
FT   NP_BIND      25     32       ATP. {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
//
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