ID ADDA_CLOB8 Reviewed; 1245 AA.
AC A6LPC4;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 95.
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=5.6.2.4 {ECO:0000255|HAMAP-Rule:MF_01451};
DE AltName: Full=ATP-dependent helicase/nuclease AddA {ECO:0000255|HAMAP-Rule:MF_01451};
DE AltName: Full=DNA 3'-5' helicase AddA {ECO:0000255|HAMAP-Rule:MF_01451};
GN Name=addA {ECO:0000255|HAMAP-Rule:MF_01451}; OrderedLocusNames=Cbei_0014;
OS Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium
OS acetobutylicum).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=290402;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51743 / NCIMB 8052;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Tapia R., Brainard J., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bennet G.,
RA Cann I., Chen J.-S., Contreras A.L., Jones D., Kashket E., Mitchell W.,
RA Stoddard S., Schwarz W., Qureshi N., Young M., Shi Z., Ezeji T., White B.,
RA Blaschek H., Richardson P.;
RT "Complete sequence of Clostridium beijerinckii NCIMB 8052.";
RL Submitted (JUN-2007) 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:0000255|HAMAP-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: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=5.6.2.4;
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; CP000721; ABR32204.1; -; Genomic_DNA.
DR RefSeq; WP_011967379.1; NC_009617.1.
DR AlphaFoldDB; A6LPC4; -.
DR SMR; A6LPC4; -.
DR KEGG; cbe:Cbei_0014; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR Proteomes; UP000000565; 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; 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; DNA damage; DNA repair; DNA-binding; Exonuclease; Helicase;
KW Hydrolase; Isomerase; Nuclease; Nucleotide-binding.
FT CHAIN 1..1245
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379248"
FT DOMAIN 4..477
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 517..815
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1245 AA; 144478 MW; 28F44FDD93C4D845 CRC64;
MGNTKWTDEQ LSAIETRNCN LLVAAAAGSG KTAVLVERII RIITNEENPV DIDKLLVVTF
TNAAAAEMRE RIADAISKEL ENNPRSKNLQ RQLTLLNRAN ITTMHSFCLD VIKNNYHRID
LDPSFRIGDQ TEGILIKSEV IEELFEDKYE EEDIGFTNLV EIFSSYKNDN NLKNLVLDLY
NFTMSGPWPE KWLINSAEAF NIKQLDELDR TNWVRVLAQS VKIELDGYVK MLEKAIEVTS
KTDGLEPYMD NLLMELSYIK KAYESTDNGL EAMFNSLSSV QFSRLKSIKK DKVSDELSQN
TVKKIRDDVK KGISELLNNA YSVNPQQMLR NIQGSYPYIK KLIELVLEFS ARFSKRKRER
NILDFNDLEH LCLKILSDYD DENNIIPSSI AMNFKEYFDE VLVDEYQDSN NVQETIINLV
SRKNDDNPNV FMVGDVKQSI YRFRQAKPEL FIEKYNTYDS SNGVNRKIQL YKNFRSRREI
IDGVNYIFKE VMSEVVGELE YTDEEALNLG ADFKENKFKD TIVGGPIEVN IIDKSHNETV
VEDNEEQEEI NNVILEGRIV AKRIKELMSK SEDEQIFKVL DKESGEYRPL KYRDIVILLR
ATKNWSEPLL DELSAEGIPV YADTGSGYFE SIEIRTIISL LKVVDNPMQD IPVISVMRSP
IMGFSAEEIS DIRLVKKDNY FYENIKYISE EAYNSINESY SDVLIAKCKY FINSVDKWRN
KSIYMAIDEF IWYLYMDTAY YGYVGAMPNG VLRQANLKIL FQRARQFEKT SFKGLFNFIN
FINKLIKSSG DMGSAQVLGE NEDVVRIMSI HKSKGLEFPV VFLCGLGKNF NLMDLNKSIL
YHDELGLGPD FIDIGKRFSI GTLAKESIKK KMKFETLSEE MRILYVACTR AKEKLIMTGT
VGNLEKSAEK WLGSASLDYN RISPSEVLKG KSYLDWICMS LCQHRDGSVL SESFGTENLI
LKDDNSRWKV SFWNKGDLID KTKTEVLEQG EGYELTIINN KPYDNYLYEE VDKILSYKYP
FKASTTIKSN ISVSDLKRRH AEEDYDTEQL YREKVKVVPK FLQEKKGLTP SEKGTAVHFV
MKKIDFNRVS STEEIKEQLH ELFEKEFLLS EELKVINPTK ILSFFRSDLG KKILDLNCRG
EKIYREIPFY TEISSLEVDK TLDNIYKDEK IRLQGIIDCF FEYKGDIILI DYKTDYIMEG
HEDEFKEKYR KQLDYYSDAI FKLTGKKVKY KYLYSFYLEK EIKII
//
