ADDA_LYSSC
ID ADDA_LYSSC Reviewed; 1238 AA.
AC B1HN90;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=ATP-dependent helicase/nuclease subunit A {ECO:0000255|HAMAP-Rule:MF_01451};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01451};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01451};
DE AltName: Full=ATP-dependent helicase/nuclease AddA {ECO:0000255|HAMAP-Rule:MF_01451};
GN Name=addA {ECO:0000255|HAMAP-Rule:MF_01451}; OrderedLocusNames=Bsph_1199;
OS Lysinibacillus sphaericus (strain C3-41).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=444177;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3-41;
RX PubMed=18296527; DOI=10.1128/jb.01652-07;
RA Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M.,
RA Berry C., Yuan Z.;
RT "Complete genome sequence of the mosquitocidal bacterium Bacillus
RT sphaericus C3-41 and comparison with those of closely related Bacillus
RT species.";
RL J. Bacteriol. 190:2892-2902(2008).
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:0000255|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=3.6.4.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01451};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01451};
CC -!- SUBUNIT: Heterodimer of AddA and AddB/RexB. {ECO:0000255|HAMAP-
CC Rule:MF_01451}.
CC -!- SIMILARITY: Belongs to the helicase family. AddA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01451}.
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DR EMBL; CP000817; ACA38807.1; -; Genomic_DNA.
DR RefSeq; WP_012292938.1; NC_010382.1.
DR AlphaFoldDB; B1HN90; -.
DR SMR; B1HN90; -.
DR PRIDE; B1HN90; -.
DR EnsemblBacteria; ACA38807; ACA38807; Bsph_1199.
DR KEGG; lsp:Bsph_1199; -.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000002164; 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:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 4.
DR Gene3D; 3.90.320.10; -; 1.
DR HAMAP; MF_01451; AddA; 1.
DR InterPro; IPR014152; DNA_helicase_suAddA.
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 PANTHER; PTHR11070; PTHR11070; 1.
DR PANTHER; PTHR11070:SF48; PTHR11070:SF48; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
DR TIGRFAMs; TIGR02785; addA_Gpos; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Exonuclease; Helicase;
KW Hydrolase; Nuclease; Nucleotide-binding.
FT CHAIN 1..1238
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379300"
FT DOMAIN 12..490
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 510..818
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1238 AA; 142526 MW; 05E79C8B23FFE63C CRC64;
MVQTIPIKPA DVSWTDDQWK AIYASGQDTL VSAAAGSGKT AVLINRMIEK VIATDNPINV
DELLVVTFTN ASAAEMRHRM SEALEKAIVE NPTSSHLRRQ LSLINKAQIS TLHSFCLAIV
KQYAYLLDID PGFRIANEAE VALLRDDIVA DVLEGAYDSE EETQVQAIYR LVDSFTSDRD
DQAIETLISK LYDTSRVHAE PQRWLWSLPK AYELAEEVTI DDLELSHYVK LTVRHSLEEA
FVLISEMRAI TLQPDGPAPY AETAEIDFAM IQEGIRISQE GTWQELFDYF ATVKWSTLKR
VSKDALVDVE LQELAKKKRE AAKKIMNKMK ETYFIRTPAR LLEEIRLMAP IIGTLVELTT
IFSEQFRLAK LERGIIDFSD LEHYALQILT VEVDGELQPS PVALDLKKRF KEVLVDEYQD
TNMLQETILQ LVKSGEEQDG NLFMVGDVKQ SIYRFRLAEP KLFMRKYSEF LETPDATGMR
IDLNANFRSR KEVLNVTNYI FAQIMGERVG EILYDDNASL KPAAPYDEKE VPVELVVMHP
PQDEETVDEQ EDKTDEASEL EELKKSQYEA RFIIDRIRQM MEDGTTVYDT KSMTERPLKY
SDIVILMRSM TWSTDLVEEF KLAGIPLYAE SSKGYFDALE VMIILNVLKV VDNPYQDIPL
ASVLRAPFVG LTENELAKIR LADSKVPFYD ALRQFIRSEG QGVQTTTFEK LQRFMLAFEN
WRDLARRGSL SDLIWKIYLD THYYEMVGAM PNGKQRQANL RILHDRALMY EQTAFRGLFR
FLRFIDRMRT RGDDLGTAKS IGEKDDVVRL VTIHSSKGLE YPVVFVAGMG RPFNKMDFHH
PYLFDQDFGL AVKAIDPENR ITYTSLPFLA LKEKKELEMR AEEMRVLYVA MTRAKERLIL
VGSVKNWEKT RDNWQDAQNI PSDAPLQEYL RARANSYLDW IGPAVARHGD FASQATTSYK
ELDSPSHWWI QPIDTRHYSY DIQAFNDEIQ QHLTTQEDEA LLSEIKARFH AQYTYQKSTR
KRSKTSVSEI KRLENLQRQE EPEYYFATPA KRTSTSIAPR PTFLQDQQLT GTEIGTAVHT
VMQHIPQFGF DTIEAVKGFV ANLVAKQLLT EAEGKVVPIK KVYHFFHTEI GQRFKQARQI
RREMPFTISR VDEDGDAQIV QGIIDCLFED EYGNWVLLDY KTDRILPHFA KEPALTKEIM
GRYAVQLRVY SEAIESILQI KVSEKVLYLF DNEQTVQA
