ID J8ZL77_ENTFC Unreviewed; 1240 AA.
AC J8ZL77;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
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=HMPREF1345_01085 {ECO:0000313|EMBL:EJV54794.1};
OS Enterococcus faecium TX1337RF.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1134802 {ECO:0000313|EMBL:EJV54794.1, ECO:0000313|Proteomes:UP000003117};
RN [1] {ECO:0000313|EMBL:EJV54794.1, ECO:0000313|Proteomes:UP000003117}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX1337RF {ECO:0000313|EMBL:EJV54794.1,
RC ECO:0000313|Proteomes:UP000003117};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (APR-2012) 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 -!- 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:EJV54794.1}.
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DR EMBL; AMAA01000039; EJV54794.1; -; Genomic_DNA.
DR RefSeq; WP_002313817.1; NZ_JH804716.1.
DR AlphaFoldDB; J8ZL77; -.
DR PATRIC; fig|1134802.3.peg.1010; -.
DR HOGENOM; CLU_001114_3_1_9; -.
DR Proteomes; UP000003117; 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; 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}.
FT DOMAIN 11..480
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 507..798
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT COILED 62..89
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1240 AA; 144298 MW; 45C8F3E07FD13679 CRC64;
MNQIPLKPQN ERFTDDQWQA IFDQGDNLLV SASAGSGKTT VLVRRVIEKL KMGFDIDELL
IVTFTEAAAR EMKERIQEAL QEAVNSESDP VRRQHFTKQL VLLPTANIST LHAFCLTVIR
RYYYLIDIDP VFRMLTDETE TILMKEDVWD ELREALYAEN DERFFQLTMN FSNDRSDDGL
TNLVFSLYEF ARANPDPKKW LEQLSANYRL TEGLAKSRLY QEQIRPLVLA DVYQCVQLYE
QMTQLAQGEG LEKMHEQVAG EQQQIKNIYE AFSQDRLEDA YASLEQLTFS TFKSSRKAEL
KEISNEVKGM RDKAKKLIQQ ISKSYFPVSP SQMEELTEKA LPLVEEMTKV TQSFMDGFSM
RKREKGVLDF NDLEHLALQI LTEKTKDAWL PSEASKHYRK KFKEVMVDEY QDVNQLQEAI
LYWLREPDDT KGNMFMVGDV KQSIYSFRLA DPSLFIGKYE NFSKKEGGRR IVLAENFRSR
KEVLSFTNLI FEQLMDPAVG QINYDEAAKL IQGFSDFPEN EQFEPEIMIY EKEQEESEIE
IPTDDILEDK TEGELFMTGL KIRQLIDSSF MIYDKKSKKD RPIEYRDIVL LTPTKKNNLT
ILEIFKTLDI PLEMNDAQNY FQATEIRTMI SLLQLIDNPY QDIPLAAVLR SPVVGLIEPE
LASIRLADRA HTYYDAVLAY QASNEDELAV KLEHFGKQLD HWRELARRSS ITDLLWDIYY
ETGYLEYVVG LPAGAQRQAN LYALVDRAKA YEQSSFRGLY QFVRFIEKMQ EKDKDLAEPV
ISIEDNAVRV MTIHASKGLE FPVVFLLDMT KEFNLQDLRN RYAFEEKLGA GIRYMDPETR
VLYDTLPFQA IKLAKQNKLL SEEMRKLYVG LTRAEQKLFI VGSYKNKEQM IQTWSEAADH
EELVFDPELR LKGRSSLMNW IGYGLIRHPE MQKYLEEEVS TSLLQYSNAQ FSISWMNQQS
IIEQRQLLAE KELVNLDQQV KEKETVLADS LQKRLAYEYP YQASSQTTSY QSVSEIKRLF
EDPDDTQESR LTLESSQTKA ASRQFRYTQE QLAEPKFLQK DRQVSAAAVG TATHALLQLL
PLEMPTTESI NQKLQELVKK RLIDEKVAKK VDVSSIIWFF QTELGQQLIA NKENVKREQP
FSMLLSADEV FQDYPNQEDE LLIHGIVDGY LEEKDHLHIY DFKTDFILHP DDPAEIDAIV
QKYQGQLRLY QQAMTEALNK PVENVFLILL RVKRIININK
//
