ID A0A0R1MC71_9LACO Unreviewed; 1241 AA.
AC A0A0R1MC71;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=ATP-dependent helicase/nuclease subunit A {ECO:0000256|HAMAP-Rule:MF_01451};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01451};
DE EC=5.6.2.4 {ECO:0000256|HAMAP-Rule:MF_01451};
DE AltName: Full=ATP-dependent helicase/nuclease AddA {ECO:0000256|HAMAP-Rule:MF_01451};
DE AltName: Full=DNA 3'-5' helicase AddA {ECO:0000256|HAMAP-Rule:MF_01451};
GN Name=addA {ECO:0000256|HAMAP-Rule:MF_01451};
GN ORFNames=FD46_GL000423 {ECO:0000313|EMBL:KRL05676.1};
OS Liquorilactobacillus oeni DSM 19972.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1423777 {ECO:0000313|EMBL:KRL05676.1, ECO:0000313|Proteomes:UP000051686};
RN [1] {ECO:0000313|EMBL:KRL05676.1, ECO:0000313|Proteomes:UP000051686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19972 {ECO:0000313|EMBL:KRL05676.1,
RC ECO:0000313|Proteomes:UP000051686};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:0000256|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=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618, ECO:0000256|HAMAP-
CC Rule:MF_01451};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01451};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01451};
CC -!- SUBUNIT: Heterodimer of AddA and AddB/RexB. {ECO:0000256|HAMAP-
CC Rule:MF_01451}.
CC -!- SIMILARITY: Belongs to the helicase family. AddA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01451}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRL05676.1}.
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DR EMBL; AZEH01000020; KRL05676.1; -; Genomic_DNA.
DR RefSeq; WP_057895419.1; NZ_AZEH01000020.1.
DR AlphaFoldDB; A0A0R1MC71; -.
DR STRING; 1423777.FD46_GL000423; -.
DR PATRIC; fig|1423777.3.peg.444; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000051686; Unassembled WGS sequence.
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:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR CDD; cd17932; DEXQc_UvrD; 2.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR HAMAP; MF_01451; AddA; 1.
DR InterPro; IPR014152; AddA.
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 NCBIfam; TIGR02785; addA_Gpos; 1.
DR PANTHER; PTHR11070:SF48; ATP-DEPENDENT HELICASE_NUCLEASE SUBUNIT A; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01451}; Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01451};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01451};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01451};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01451};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01451}; Reference proteome {ECO:0000313|Proteomes:UP000051686}.
FT DOMAIN 4..470
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 497..799
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT COILED 244..308
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1241 AA; 143001 MW; 484FDF7E19E1CA22 CRC64;
MAKINFTPAQ KEAIEEKSGN ILVSASAGSG KTRVLVERVL HHLRSGIGID EMLIVTFTEA
AAEEMRERIQ SALQKEVSTA PVEKKQWYVT QLTKLNTANI STLHAFCLHL IQRYYYIIGL
DPVFRLLSDD TERELLREDV WNEVREEFYG QKDELFEQLA QNFSNDRSDE GLTDVVFRTF
DFAGAKADSA SWLHQIPTIY QNENENLTES SLYKKKLVPI LTERLKQAEA VFEAAAGIAK
NYSLSKFEET LKKDQEMVEE LLQKLQTESW NTLRNIFQNL TFQRAPQLRK LEDEQKKAKD
ELLGLRNAAK KVVNDLNDKY FLLDEKQIKD VLQESQKLVT ELMRVVVSFS EAFTAEKRQR
HLLDFNDLEH LALKILQGKT PESRQVQENL QQKFSEILVD EYQDTNQLQE TLISRLVGTA
GNLFMVGDVK QSIYGFRLAD PALFLRKYHA YAQAESNGKR IILAENFRSV KDITAFSNLI
FMQLMDKQVG GLDYDKNAQL KYGANYYPPM KTETEVLIYE SETKEESKKE KEPFDESFTV
DNAAEGQVLV AVQKIKRLLA ENKKIYDRKL GEKRNVQFGD IVLLVPTRNN NLLIMSEFQK
AGLPVYIKDA QNYFQTTEIQ IMLSLLKIID NPYQDIPLVS VLRSPIVGLK ENALAYLRIN
KKTGDYYQAV KTFQKNFDPR KENDFGQRVY EKVGKFLRML TSFRDLAHQN QLADLIWEIY
DQTGFLDYVG GMPGGAQRQA NLHALYERAS EYEKMSFRGL FQFIRFVNKL QKRDQDLAEA
NSKVAQDAVQ VMTIHGSKGL EFPIVFLMDA TRQFNERALK EDYLLDDTQG LGITLLLPKE
RIKVDTLPKL IINEHKQRQN AAEQMRLLYV ALTRAEQQLY IVGTYRTKKE AVSKWKQAFQ
AEGVTLGSSL RQETKCFMDW IGMCLIRRSE TQAQFGLEQP KLAELEKNTA HFKISFFTQG
ELKPAQKQEG ADWLKQLESK KGNVFDSQTE QVFQKAAVIL NYSYPNDELT KTTAYQSVSD
IKRLFSDPDE SELTHLDDWN RLQTPTRGHR IVQSEFRLPQ FMEQKEYVTS AQVGTATHEL
LRQVSLKQEP TIAELTNQLK KLETQKVIER AVAQKVNIQH VRRFFKSSLG QLLLKNSENV
KREVPFSALI PAKKLFSTIE TNNDILLHGI IDGYVDTKTQ VVVFDYKTDF LLPEDIEKKK
ELTARYQGQL NLYALALESI LGKKIDHKYL YLLATGQVVE V
//
