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Database: UniProt
Entry: Q9CJI9
LinkDB: Q9CJI9
Original site: Q9CJI9 
ID   ADDA_LACLA              Reviewed;        1203 AA.
AC   Q9CJI9;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   05-DEC-2018, entry version 98.
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}; Synonyms=rexA;
GN   OrderedLocusNames=LL0004; ORFNames=L025, L0251;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus
OS   lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.GR-1697R;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K.,
RA   Weissenbach J., Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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; AE005176; AAK04102.1; -; Genomic_DNA.
DR   PIR; D86625; D86625.
DR   RefSeq; NP_266160.1; NC_002662.1.
DR   RefSeq; WP_010905024.1; NC_002662.1.
DR   ProteinModelPortal; Q9CJI9; -.
DR   SMR; Q9CJI9; -.
DR   STRING; 272623.L0251; -.
DR   PaxDb; Q9CJI9; -.
DR   EnsemblBacteria; AAK04102; AAK04102; L0251.
DR   GeneID; 1113602; -.
DR   KEGG; lla:L0251; -.
DR   PATRIC; fig|272623.7.peg.4; -.
DR   eggNOG; ENOG4107R2I; Bacteria.
DR   eggNOG; COG1074; LUCA.
DR   HOGENOM; HOG000285114; -.
DR   KO; K16898; -.
DR   OMA; KQSIYRW; -.
DR   BioCyc; LLAC272623:L0251-MONOMER; -.
DR   Proteomes; UP000002196; 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; 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; 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;
KW   Reference proteome.
FT   CHAIN         1   1203       ATP-dependent helicase/nuclease subunit
FT                                A.
FT                                /FTId=PRO_0000379292.
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;  138634 MW;  9AC0DF6A331F370D CRC64;
     MSEVKLTPEQ NEAIHSSGKN ILVSASAGSG KTFVMAQRIV EKVKQGIEID RLFISTFTKK
     AASELRMRLE RDLKKARQES SDENQACRLT LALQNLSNAD IGTMDSFTQK LTKTNFNRVN
     IDPNFRILAD QTESDLIRQE VFEQLVESYL SGDDGLNISK EKFEELIKNF SKDRNIAGFQ
     KVVYTIYRFA SATENPIKWL ENQFLKGFET YKSLIDLSAD FSADIKENLL IFFELLETSL
     TNGVVAKKGA GRDKANLILD NKNELLEAIT TKDFATFTEL FLSIDTDIRV GSSKDEILSA
     LKKDFSVQKQ DLVGSKSKPG EIRKFVDKIK HGQLIEKYQN QAFEIAENLQ KFVIEFYQSY
     LERKKNENAF EYSDIAHFAI EILEENPDIR ETLREHYDEI MIDEYQDTSH TQERMLELLS
     NGHNLFMVGD IKQSIYGFRL ADPGLFLEKY KDYAKTENPN QLIRLKENFR SRGEVLTFTN
     DIFKHLMDEK LGEMTYGKEE ALVQGNITDY PVESEKDFYP ELLLYKENTS DEETDESEVR
     ISDGEIKGAA QEIKKLIEAG VEPKDIAILV RSKSNNNKIE DILLSYDIPV VLDEGRVDFL
     KSMEVLIMLD VLRAIDNPLY DLSLVAMLRS PLFGFNEDEL TRISTQGSHD LRFWDKILLS
     LNKEGQNPEL INPSLENKLK AFYKKFTEWR KLVNQVAIHD LLWKIYTETY YFDYVGALKN
     GEIRQANLQA LAVRAESYES SGYKGLFKFV RLINKFMEQN NDLASVNIKL PQSAVRVMTF
     HKSKGLEFDY VFLMNLQSRF NDRDLKENVI LSRENGLGMK LIADLKDEAD VITDFPYALV
     KMETFPYMVN KDLKQRAALS EEMRVLYVAF TRAKKKLYLV GKIKETDKKS GLDLYDNASL
     EGKILEDKFR NSSRGFQHWI LALQNATKLP IKLNVYTKEE LEAEKLEFTS QPDFKKLVEE
     SEKFDNIMAH SDEIQKAQKI MNYEYPHQAA TELSSIQTPS QVKKRSYEKQ LQVGEIQPKS
     EFTRVKKLDF SDFGPKKVTA AEIGSATHSF MQYADFSQAD LFSFQATLDE MGFDEKIKNQ
     IDIAKILTLF DTDFGQFLSE NVDKTVKEAP FSMLRTDEFA KEQYIVRGIC DGFVKLTDKI
     VLFDYKTDRF TSSSAISEIK ERYRDQMNLY SEALKKAYDV NQVDKYLILL GGPQQVFVEK
     LDD
//
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