ID A0A133Q8E3_STALU Unreviewed; 1216 AA.
AC A0A133Q8E3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=HMPREF3225_00750 {ECO:0000313|EMBL:KXA39119.1};
OS Staphylococcus lugdunensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=28035 {ECO:0000313|EMBL:KXA39119.1, ECO:0000313|Proteomes:UP000070063};
RN [1] {ECO:0000313|EMBL:KXA39119.1, ECO:0000313|Proteomes:UP000070063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJR7738 {ECO:0000313|EMBL:KXA39119.1,
RC ECO:0000313|Proteomes:UP000070063};
RA Oliw E.H.;
RL Submitted (JAN-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}.
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:KXA39119.1}.
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DR EMBL; LRQI01000029; KXA39119.1; -; Genomic_DNA.
DR RefSeq; WP_002459534.1; NZ_LS483312.1.
DR AlphaFoldDB; A0A133Q8E3; -.
DR STRING; 28035.B6N84_09440; -.
DR PATRIC; fig|28035.7.peg.760; -.
DR eggNOG; COG1074; Bacteria.
DR Proteomes; UP000070063; 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 9..474
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 495..785
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1216 AA; 141902 MW; A48E9A07F6FC0399 CRC64;
MIPVKPEGVI WTDAQWQSIY AKGQDVLVAA AAGSGKTAVL VERIIQRIIR DNVDVDRLLV
VTFTNLSARE MKHRVEQRIQ EAALEDPNNT HLKNQRIKIH QAQISTLHSF CLKLIQQHYD
VLDVDPNFRT SSEAENILLL EQTIDETLEH YYDVLNSDFI ELAEQLSKDR NDDDFRTIIK
SLYYFSIANP NPFEWLTQLV KPYQNEAQQD NLLQLLTDLS RIFLRAAQEV LSKSYEIFTL
AEDTDKQIAV IEDEMAFMTK AFDGDMIQSD VIANHEFVSR FPALTKKIKE VNETMGDALV
EAKAYYDKYK SLVSKVQADY FSRSAQDLKR DMQRLAPRVN ILADIVKDVI TAFGQKKRSR
NILDFADYEH FALQILTNDD GSPSHIAEMY REQFAEILVD EYQDTNRVQE QILSCIKTGS
EADGNLFMVG DVKQSIYKFR QADPSLFIEK YQRFNAEGNG TGIRIDLSQN FRSRKEVLST
TNYLFKHMMD EEVGEISYDD AAQLYYGAPF DEVDHPVELR TLIEANKEHS ELNGSEQEAE
YIVKQVKDIL ENKRIFDMKT GHYRQPTYKD IVILERSFSQ ARDLQQAFKD HDIPFHVNSR
QGYFEQTEVR LVLSFLRTID NPLQDIYLVG LMRSVIYQFT EDELANIRVF SPNDDYFYQS
IVNYINHDLA NKKLVKKLQN FIADIKMYQI YSQSNPVYQL IDKFYHDHYV IQYFSGLIGG
KGRRANLYGL FNKAIEFENS SFRGLYQFIR FIDELIDRGQ DFGEENIVGP NDNVVKMMTI
HSSKGLEFPF VIYSGLTREF NKKDLREQVI LNQKYGLGID YYDIDKNMAY PSLSSVAYKA
ITEKEMISEE MRLIYVALTR AKEQLILIGR LKSTKKLEEY EKLAISGSHI AINERLTAEH
PFELIYGILS KHKSYELTPD LMFENDIANL AENIRPNVNI IIDYFEDIIE ANHQDMNEQR
SISDLNTLDT GNDDIKAKIT QQLKFKYPNV INTTKPSKQS VSELKRQLET EESDTNYDRV
RQYRIGVATY ERPRFMRHVT KRKANEVGTL MHTVMQHLPF KPKRMTEEAL EQYIDHLITQ
QIIEHDAKKD IKFPEIMTFI QSDLYLEIAE AEQIYRELPF VVNQAKVDNI SDNHEDVAII
QGMIDLIYKK DNQYYFVDYK TDAFNRRKGM TDEEIGEQLK EKYRIQMQYY KNALETMLHT
EVKGSLYFFQ FGRLSI
//
