ID C2NEB4_BACCE Unreviewed; 1166 AA.
AC C2NEB4;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 81.
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=bcere0004_10170 {ECO:0000313|EMBL:EEK57623.1};
OS Bacillus cereus BGSC 6E1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=526970 {ECO:0000313|EMBL:EEK57623.1};
RN [1] {ECO:0000313|EMBL:EEK57623.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGSC 6E1 {ECO:0000313|EMBL:EEK57623.1};
RX PubMed=22645259; DOI=10.1101/gr.134437.111;
RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A.,
RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K.,
RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.;
RT "Genomic characterization of the Bacillus cereus sensu lato species:
RT Backdrop to the evolution of Bacillus anthracis.";
RL Genome Res. 22:1512-1524(2012).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00560}.
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:EEK57623.1}.
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DR EMBL; ACLU01000030; EEK57623.1; -; Genomic_DNA.
DR AlphaFoldDB; C2NEB4; -.
DR HOGENOM; CLU_001114_3_1_9; -.
DR Proteomes; UP000000284; Chromosome.
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; cd18807; SF1_C_UvrD; 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; 3.
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 1..410
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 430..730
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
SQ SEQUENCE 1166 AA; 134527 MW; BD09FDB164B40077 CRC64;
MKNRIGEALE KVLIDEPGYQ HVRKQLSLLN KASISTIHSF CLQVIRGYYY MLDVDPRFRI
ANQTENELLK EEVLDDILEE EYGIEDNTIF FELVDRYTSD RSDDDLQRMI LALHTESRAH
PNPEKWLDKL VEAYDVEGKT IEDLVYASYL LEDVKFQLET AEQHIRKATE LAMLPDGPAP
RIETLQADLA LLGTLSSAAR ESWTSVYEAM QNVSWQTLKR IKKSDYNEDI VKQVDSLRNK
AKDEVKKLQE ELFSRRPESF LRDFQDMHPV LEKLVQLVKV FTERFQAMKR DKGMVDFTDL
EHFCLQILSE QSEDGEMKPS AVALQYRNKF AEVLVDEYQD TNFVQESIIK FVTKDSESEG
NLFMVGDVKQ SIYRFRLAEP GLFLGKYKRF TQEGLGGGMK IDLAKNFRSR HEVLAGTNFI
FKQIMGEEVG EIDYDADAEL KLGASYPEGE DVAAELLCIQ QTEEEVIDGE EGAEVEKAQL
EARLMAQRIK AMVDSGYEVY DRKTDSMRPV QYRDFVILLR SMPWAPQIME ELKLQGIPVY
ADLATGYFEA TEVNIMMNVF RVIDNPMQDI PLAAVLRSPI VGLNDEELAT LRAHGKKGSF
YEVMSSFLKG APLEEEKELH DKLEWFYNLL QGWREFARQQ SLSDLIWKVY GETGYYDFVG
GLPAGKQRQA NLRVLYDRAR QYEATSFRGL FRFLRFIERI LERGDDMGTA RALGEQEDVV
RIMTIHKSKG LEFPVVFVAG LGRRFNTQDL MKRFLLHKDF GFGSQFIDPR KRIKYTTLSQ
LAIKRKMKME LIAEEMRVLY VALTRAKEKL ILIGTVKDAT KEMEKWLDAR EHSEWLLPDH
VRAGASCYLD WIAPSLYRHR DSEMLLELGQ GSIPDEIYGY DTSWKVEVVD GNTLLAPEPV
QEEKQELLEA LREKKAVPLQ SERKDEVYDR LMWKYGYEEA TSHRAKQSVT EIKRNYQSEE
GSDNAFIKKL RAPIKTRPRF MEKKGLTYAE RGTAVHAVMQ HVDLKKPITV EVLQEQIAGM
VNKELLTFEQ AEEIAVEKVI SFFDSDLGKR VLAAKSVERE VPFTMMLAAE EAYQDWQGES
GESILVQGVI DCMIEEEDGI TLIDFKTDTI EGKFPGGFEQ AKPILETRYK VQLSLYAKAL
EKSLQHPVKE KCLYFFDGNH VIKVEE
//
