ID A0A1I1R4F4_9LACO Unreviewed; 1203 AA.
AC A0A1I1R4F4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=SAMN04487792_0144 {ECO:0000313|EMBL:SFD29261.1};
OS Lactobacillus bombicola.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1505723 {ECO:0000313|EMBL:SFD29261.1, ECO:0000313|Proteomes:UP000199599};
RN [1] {ECO:0000313|Proteomes:UP000199599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R-53102 {ECO:0000313|Proteomes:UP000199599};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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: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}.
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DR EMBL; FOMN01000001; SFD29261.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1R4F4; -.
DR STRING; 1505723.SAMN04487792_0144; -.
DR Proteomes; UP000199599; 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; 1.
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};
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}.
FT DOMAIN 2..471
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 498..782
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 23..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1203 AA; 139684 MW; 36FFEDED8005C6CC CRC64;
MTSYTNQQKQ AITLKEHDIL VSASAGSGKT TVLVQRLLQE ILGGISVDQL LVVTFTKAAA
QEMKNRIKMI IQAELNQTTE PSKQRYLRQQ LNLIDAANIS TIDAFCLDII HRFYYVIDLD
PSFSILTDET QASLMRERAL HEIENEFLTN NDEDFLAFYN NFAGDRDAET ARNLLLDLYN
YAMAKPDYTA WLKNLPQKYQ VKANLITSPL WQEQVKPYLF ESFSTLREKI NHYLSTSIIE
TKELKKVKES FTLFKRGLDN YLTSLKQDYD YDLQRENLRS CEFSRFNKSQ KWDEDILDFI
DECAELKSEA NTLVFNSFTS FYATDEQEQL SILKQGQQIM LGITKAETAL INRFNELKRA
QNLLDYSDME QLAYQILSQD TSSSAMARSF YQNKFKEIMV DEYQDINQLQ ENILQLIKKD
KHNTLFMVGD VKQSIYGFRQ ADPSLFLRKY EETVENKTQK RILLADNFRS TKPIIKIVNQ
VFDNILTPDF GGIDYAKEGE LTFGAQYYPA DLAQATEFLY YQTEDDKEND EQTFDSTEIA
MIISRIKQFK QENLQIYDVK AGQKRPFKYS DIAIITRSRS DNLAMMQEFA NENIPLLVTD
AKNYFQTIEL TIIMNYLRLI DNPDQDIPLV TVLRSPLFNF KEPDLAKIRI NSKKVTFYNA
LTAYVAINDE LSQKIKIFLN QLASLRQFAV NHRISELIWS IYERTDLLEI MTALPNGKQR
RINLESLYER ASSYESAGFK GLYQFINFIE RMRRSQKDLA QPLLTNEVDD SVKLMTIHGS
KGLEFPIVFY AGLHHRFQKR DISGDYIITA DNVGLTIQRN HYCADTLLKA IDNMTKEKQL
LEEEARILYV GMTRARQKLI LTAEISNFEQ NIELWHRKAK QHKISLNDKL TVTNPLGFIG
PALGLKECSS LSLNDLNMDL DLSKDFIFVN YHKQAKTVEA VHEKINTKQK ANYSPELLQR
TAQKLYDFSY TFKDASQTTA YQSVSEIKKA FNDPLDTELE NAHLLSSTNR YLQPIDTKPK
FLFKTTFTGV EIGTAMHLLL QYYDYNGRGD QEQLDEEIKD LIKHHQLNPD IVSSLNQDQI
NWFVHSDFAK EFWQKPHNLK REIEFSSLIP ASTLFSDFSD PDAKTLIHGT IDGYFIQDDG
IILFDYKTDY IDPNHQDEAI EKVKHKYTGQ LRLYEQALNS FANKKVKHKY LILLNAQKIV
EVK
//
