ADDA_LACLA
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 03-AUG-2022, entry version 111.
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 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., Weissenbach J.,
RA 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 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; 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 AlphaFoldDB; Q9CJI9; -.
DR SMR; Q9CJI9; -.
DR STRING; 272623.L0251; -.
DR PaxDb; Q9CJI9; -.
DR EnsemblBacteria; AAK04102; AAK04102; L0251.
DR KEGG; lla:L0251; -.
DR PATRIC; fig|272623.7.peg.4; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
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: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; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; -; 4.
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; 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; Reference proteome.
FT CHAIN 1..1203
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379292"
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; 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
