ID A0A1L8RI04_9ENTE Unreviewed; 1192 AA.
AC A0A1L8RI04;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=RU97_GL000971 {ECO:0000313|EMBL:OJG19400.1};
OS Enterococcus canis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=214095 {ECO:0000313|EMBL:OJG19400.1, ECO:0000313|Proteomes:UP000181884};
RN [1] {ECO:0000313|EMBL:OJG19400.1, ECO:0000313|Proteomes:UP000181884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17029 {ECO:0000313|EMBL:OJG19400.1,
RC ECO:0000313|Proteomes:UP000181884};
RA Zhong Z., Sun Z., Liu W., Zhang W., Zhang H.;
RT "Draft genome sequences of 29 type strains of Enterococci.";
RL Submitted (DEC-2014) 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}.
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922}.
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:OJG19400.1}.
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DR EMBL; JXKH01000002; OJG19400.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L8RI04; -.
DR STRING; 214095.RU97_GL000971; -.
DR Proteomes; UP000181884; 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 Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 1.10.274.50; -; 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; IPR013986; DExx_box_DNA_helicase_dom_sf.
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 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; 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:UP000181884}.
FT DOMAIN 1..452
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 477..765
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT COILED 33..60
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 267..294
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 3..10
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1192 AA; 136635 MW; 2C47257A3288C925 CRC64;
MSASAGSGKT TVLVERVIEK IIDGTNVDQL LIVTFTEAAA REMKERIQKA LQENAANTRD
PETRQRFLQQ LTLLPTANIS TLHAFCLTVI RRFYYLIDMD PVFRLLTDET ETLLLKEDVW
DDLREEWYSK QDETFFQLTA NFSNDRSDAG LTDVLFSLYD FARANPDPEG WLKGLTQAYD
TSKGLGASPL FKEYLQPNYL ENLASVQTRY QEMIRLCEGV PELKKITELA YNEAAQTTQL
QQFLEAGDLE TTYHAFSNLT FDKFPTIRKP EEAIKEVKDQ AKQLRDDNVK ALRAIQKDLF
AVDPETMTKI MAEAQTVVGN LSEVCLQFMH RYRQRKSAQG LLDFNDLEHL TLQILATLDS
EGWHASEASA FYREKFTEVL VDEYQDLNRL QEALLHWVTR TEPGNMFMVG DVKQSIYAFR
LADPTLFIEK YQHYERAEGG RRIVLAENFR SRKEVLDFTN LIFDQLMDEQ VGQIAYDEAA
KLVNGFTAFP ETATFDTEIW IYEKGVEAET ELVIEDKTEG ELRMTARRIR QLMDEGFEVY
DKKQKVNRPL RYSDIVLLTP TKKNNLAILE LFKEADIPVE VNDAQNYFQA TEIRIMVALL
QLIDNPYQDI PLAAVLRSPL VGLNEQELAE IRLANKQSSF YEALKQFLAA TESPLQAKLG
FFMEQFQTWR ELARRDSLAT LIWQIYQDTA FLDYVGGMPA GAQRQANLRA LAERAASYEK
TSFRGLFQFV RFIEKMQEKD KDLAEPVLLG GEEAVRVMTI HASKGLEFPV VFVLDLTKQF
RLSELNGNYI FDEKLGAGIR YLEPTTRTLY PTMPYLAIRQ AKLQKLLSEE MRKLYVALTR
AEQKLILVGS YQDEATAWKT WAKVAQHDQR VLPASLRLAQ GGNLMNWIGY SLIRHPHTAI
FQKEWATANI PELKAYPDSF SIHFVQADVF AEGGQTHQET VKTSPATGLE ILAAAKGRLA
FQYPYSNATE TTSYQSVSEI KRVFEDPDES ELLKIDVTTR RPINRFVQEE LPKPKFLQET
RAPLANEIGT ATHYVLQVMS LEKPTMKSLK ELVVSLVQEK RLAPQVAEKI NLQKIITFYD
SDLGQRILKE AEQVKREQPF SMLLPANRLF ADYPTADEIL VHGIVDGYID NDELVLYDFK
TDHLSGPAGR EKALERYRGQ LNVYKEALEL ATGKKVAETW LILLEPEEQI KL
//
