ID ADDA_STRR6 Reviewed; 1216 AA.
AC Q8DPR6;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 125.
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}; Synonyms=rexA;
GN OrderedLocusNames=spr1040;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
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; AE007317; AAK99844.1; -; Genomic_DNA.
DR PIR; D95133; D95133.
DR PIR; H98001; H98001.
DR RefSeq; NP_358634.1; NC_003098.1.
DR RefSeq; WP_000767212.1; NC_003098.1.
DR AlphaFoldDB; Q8DPR6; -.
DR SMR; Q8DPR6; -.
DR STRING; 171101.spr1040; -.
DR KEGG; spr:spr1040; -.
DR PATRIC; fig|171101.6.peg.1129; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0033202; C:DNA helicase complex; IBA:GO_Central.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
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: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 GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..1216
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379335"
FT DOMAIN 26..488
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 515..802
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT BINDING 47..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1216 AA; 140167 MW; 950E3CBECA4D4A95 CRC64;
MKLIPFLSEE EIQKLQEAEA NSSKEQKKTA EQIEAIYTSA QNILVSASAG SGKTFVMAER
ILDQLARGVE ISQLFISTFT VKAATELKER LEKKISKKIQ ETDDVDLKQH LGRQLADLPN
AAIGTMDSFT QKFLGKHGYL LDIAPNFRIL QNQSEQLILE NEVFHEVFEA HYQGKQKETF
SHLLKNFAGR GKDERGLRQQ VYKIYDFLQS TSNPQKWLSE SFLKGFEKAD FTSEKEKLTE
QIKQALWDLE SFFRYHLDND AKEFAKAAYL ENVQLILDEI GSLNQESDSQ AYQAVLARVV
AISKEKNGRA LTNASRKADL KPLADAYNEE RKTQFAKLGQ LSDQIAILDY QERYHGDTWK
LAKTFQSFMS DFVEAYRQRK RQENAFEFAD ISHYTIEILE NFPQVRESYQ ERFHEVMVDE
YQDTNHIQER MLELLSNGHN RFMVGDIKQS IYRFRQADPQ IFNEKFQRYA QNPQEGRLII
LKENFRSSSE VLSATNDVFE RLMDQEVGEI NYDNKHQLVF ANTKLTPNPD NKAAFLLYDK
DDTGEEEESQ TETKLTGEMR LVIKEILKLH QEKGVAFKEI ALLTSSRSRN DQILLALSEY
GIPVKTDGEQ NNYLQSLEVQ VMLDTLRVIH NPLQDYALVA LMKSPMFGFD EDELARLSLQ
KAEDKVHENL YEKLVNAQKM ASSQKGLIHT ALAEKLKQFM DILASWRLYA KTHSLYDLIW
KIYNDRFYYD YVGALPNGPA RQANLYALAL RADQFEKSNF KGLSRFIRMI DQVLEAQHDL
ASVAVAPPKD AVELMTIHKS KGLEFPYVFI LNMDQDFNKQ DSMSEVILSR QNGLGVKYIA
KMETGAVEDH YPKTIKLSIP SLTYRQNEEE LQLASYSEQM RLLYVAMTRA EKKLYLVGKG
SREKLESKEY PAAKNGKLNS NTRLQARNFQ DWLWAISKVF TKDKLNFSYR FIGEDQLTRE
AIGELETKSP LQDSSQADNR QSDTIKEALE MLKEVEVYNT LHRAAIELPS VQTPSQIKKF
YEPVMDMEGV EIAGQGQSVG KKISFDLPDF STKEKVTGAE IGSATHELMQ RIDLSQQLTL
ASLTETLKQV QTSQAVRDKI NLDKILAFFD TVLGQEILAN TDHLYREQPF SMLKRDQKSQ
EDFVVRGILD GYLLYENKIV LFDYKTDRYD EPSQLVDRYR GQLALYEEAL SRAYSIENIE
KYLILLGKDE VQVVKV
//
