ID A0A0M0LGZ9_9BACI Unreviewed; 1249 AA.
AC A0A0M0LGZ9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=AMD01_00305 {ECO:0000313|EMBL:KOO50251.1};
OS Priestia koreensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=284581 {ECO:0000313|EMBL:KOO50251.1, ECO:0000313|Proteomes:UP000037558};
RN [1] {ECO:0000313|Proteomes:UP000037558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16467 {ECO:0000313|Proteomes:UP000037558};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Fjat-14210 dsm16467.";
RL Submitted (AUG-2015) 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:KOO50251.1}.
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DR EMBL; LILC01000002; KOO50251.1; -; Genomic_DNA.
DR RefSeq; WP_053399396.1; NZ_LILC01000002.1.
DR AlphaFoldDB; A0A0M0LGZ9; -.
DR STRING; 284581.AMD01_00305; -.
DR PATRIC; fig|284581.3.peg.297; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000037558; 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 CDD; cd18807; SF1_C_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}; Reference proteome {ECO:0000313|Proteomes:UP000037558}.
FT DOMAIN 12..486
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 520..813
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1249 AA; 143192 MW; E4B4214A5BEC0A8D CRC64;
MTNDLMTKPA NSQWTDDQWK AIAASGQDIL VAAAAGSGKT AVLVERIIIK VISEQDPLDV
DRLLIVTFTN ASAAEMRTRI GEALEKQLKS NPSSLHLRRQ LSLLNRASIS TLHSFCLDVI
RKYYYAIDID PGFRIADDAE AELIREEVLE ELFEEEYSIE DNSVFFDLID RYTNDRSDAD
IQVIVRHLYE FSRSNPFPKQ WLSQLINQYD VEEDTVIDSL PFIPFLLKEV SSQLKGIQAL
LEEGMNLTKL PEGPAPRAAN FEEDLAQIDR LRSASERSFT ELHEEMQTLS FSRLKACKKG
EYDAALVEQS GDLRKKGKES LEKLQSELFA RPVHAYMGDF SNMKPVVEKL VELVNSFAER
YDAVKREKGL VDFSDLEHYC LRILREETED GQLLPSAIGK KYRQQFKEVL VDEYQDTNMV
QESLISLVTK DDEHEGNLFM VGDVKQSIYR FRLAEPFLFL SKYKRFTHEG RQGGLKIDLN
KNFRSRSQVL DATNFIFNQV MDEEVGEISY DDDAALKLGA SYPSVEGMET ELALITKDKK
GASDEESPDE GVFSEAELET SQLEARYMAR RIKKMVQERF QIYDRKLETT RSVTYRDFVI
LLRSMPWAPQ IMEEFKEEGV PIYANLSTGY FDATEVSIML SLLRVIDNPY QDIPLAAILR
SPIVGLSEEE LATIRIANKK GLFYEAMQDF QRQVASAEQA ELEEKVNLFY QQLQTWRTRA
RQDSLSSLIW QIYRDTGFYD FVGGLPGGKQ RQANLRALHD RARQYEATSF RGLFRFLRFI
ERMQERGDDL GAARALGEQE DLVRLMTIHG SKGLEFPVVF VAGLSKQFNM MDLNKNYLLD
KELGFGSKLI NAKLRISYPT LLQQTIKRKM KNESMAEEMR VLYVALTRAK EKLILVGTVN
DIEKSVTKWE AASASSKWVL PAHLRSGAKS YLDWVGPSLI RHPSIEHLAG ERSSNVTTSP
IYNDSSKWSI QLLHAQELEE NLQEEQLQHE ALLEAVEKGE KVDIKSSFET EIHERMNWTY
SHKEAAGHYA KQSVSELKHQ QLQDGTSDER FVRKFQGPVA DRPSFMQEKT LTPAEKGTIT
HLVLQHIDLK ADVSEESVRE LVSSLITKEI LTADQAEGVN IQNVVRFLES EIGSRLRQAP
YVKRELPFRL GLKAEEIYSD WQGDTEETVL IQGVIDCLFR DEKGFVLVDF KTDNISERFG
GDFSEAKPVL QERYQFQIDT YSKAIERILK QESIERCLYF LDGGYELYL
//
