ADDA_LACCB
ID ADDA_LACCB Reviewed; 1234 AA.
AC B3WEJ1;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=LCABL_17110;
OS Lacticaseibacillus casei (strain BL23) (Lactobacillus casei).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=543734;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BL23;
RA Maze A., Boel G., Bourand A., Loux V., Gibrat J.F., Zuniga M., Hartke A.,
RA Deutscher J.;
RT "Lactobacillus casei BL23 complete genome sequence.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; FM177140; CAQ66792.1; -; Genomic_DNA.
DR RefSeq; WP_012491616.1; NC_010999.1.
DR AlphaFoldDB; B3WEJ1; -.
DR SMR; B3WEJ1; -.
DR KEGG; lcb:LCABL_17110; -.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR OrthoDB; 137860at2; -.
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.
FT CHAIN 1..1234
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379278"
FT DOMAIN 2..475
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 507..806
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT BINDING 23..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1234 AA; 136943 MW; 437591E59EF50122 CRC64;
MTQFTTSQQA AITHDGHDVL VSASAGSGKT TVLVERIIQK ILKQHADITR MLIVTFTRAA
TAEMRTKIQT ALKKALTERR HELSGEDRRH LANQIAMVNA AKISTLDAFS LQIVQTYYYV
IDLDPGFRLL TDETERYMLQ ERVWDDLREQ LYASDEAPAF EQLTANFSGD RDDSGLQDLM
FELIRQAGAT TDPKAYLEGL ATPYAPEKWE ATFSQQIWPR VKGQLLQIAT SLTQASALAN
QLPNPIWYQQ IQADLAPLQT LLETNAPTYD TVRSVLISHE FAAWSRISKG LDDADKDTKN
AAKDLRDAAK KTWQNKLAPT FALAAEQIGD LLREAQPLVA TLANVALKFE DALTAEKAAR
HVQDYSDIAH NALRILQQKD PQTGAPIADN YRASFDEVMV DEYQDISPLQ EALLAAVSTT
TPGDRFMVGD VKQSIYGFRL ADPQLFIHKY QTFQDAPTDP AAPERIILAE NFRSTKNVLA
FTNLIFSQIM DPEVGDLSYD NAAALRYGAL DYGDAHPAVK VLLYSKATSD EDSSDASELP
GDADDNEPVD IATGQTQLVL AEIQRLINDP DAQLWDRQAQ EYRRIHYRDI TLLTRQTSQN
SLIQTQFAAA GVPLFVADTK NFFKTTELMV MLALLKVIDN QKQDIPLVAV LRSPIVGLSA
DQLALIRLAA KQVPYYDAVT AFLQAEPKTP LAQRTHDMLT HFFNQLSHFR DLARENDLVT
LLWAIYQDTG FLDYVGGTPG GSQRQANLQA LIDRARTYEA GGFKGLFAFI HFITLMQKQD
QDLAMPAQVD PDNDAVKLMT IHKSKGLEFP VVFLMQANKH FNMRDQTGTA ILTKQGIGIK
WLDPETRVEY ELPQYQAAKA ARQNQTLAEE MRLLYVALTR AQQRLYVVGA TMSGNQLTSA
DKTVEKWAAA AEGEARVLAP QVRSGATSYL DWIGPALIRH PQARGLAETT IKPALVGDET
EFTIEIDVNP QVTPTATPEK VSDDSGTMVD LSAWFKKAYP FQAATTTTGF QSVSEIKRAF
DDPDTIDLVN ADRFLGPKPP MRDLTAPAFL TETPSGISPA AIGTATHLLL QLVDLAKPIT
MASLRALRDQ LTTKQVIAVD VAKHIDLTAL IRFFETDLGR LLLAKPQQVH REVPFSMLLP
ADQVFEALAD DPGEDVLIHG IIDGYVSDEQ GVTLFDYKTD HNPNTAVLVD RYRGQLNLYA
QALQDLQPKP VLHRYLVFLR TGTVVDLVAS GAGK
