ID   ADDA_STRPN              Reviewed;        1216 AA.
AC   Q97QP9;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 123.
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};
DE   AltName: Full=Exonuclease RexA;
GN   Name=addA {ECO:0000255|HAMAP-Rule:MF_01451}; Synonyms=rexA;
GN   OrderedLocusNames=SP_1152;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=R6 / R800;
RX   PubMed=15256582; DOI=10.1099/mic.0.27106-0;
RA   Halpern D., Gruss A., Claverys J.-P., El-Karoui M.;
RT   "rexAB mutants in Streptococcus pneumoniae.";
RL   Microbiology 150:2409-2414(2004).
CC   -!- FUNCTION: Involved in DNA double-strand break repair. Is not involved
CC       in recombination during natural competence or in plasmid establishment.
CC       {ECO:0000269|PubMed:15256582}.
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 RexB. {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene grow poorly, are more
CC       sensitive to UV light than wild-type cells and have reduced double-
CC       strand exonuclease activity. {ECO:0000269|PubMed:15256582}.
CC   -!- SIMILARITY: Belongs to the helicase family. AddA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01451}.
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DR   EMBL; AE005672; AAK75261.1; -; Genomic_DNA.
DR   PIR; D95133; D95133.
DR   PIR; H98001; H98001.
DR   RefSeq; WP_000767212.1; NZ_AKVY01000001.1.
DR   AlphaFoldDB; Q97QP9; -.
DR   SMR; Q97QP9; -.
DR   STRING; 170187.SP_1152; -.
DR   EnsemblBacteria; AAK75261; AAK75261; SP_1152.
DR   GeneID; 60233267; -.
DR   KEGG; spn:SP_1152; -.
DR   eggNOG; COG1074; Bacteria.
DR   OMA; KQSIYRW; -.
DR   PhylomeDB; Q97QP9; -.
DR   BioCyc; SPNE170187:G1FZB-1171-MON; -.
DR   Proteomes; UP000000585; 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; 2.
DR   PANTHER; PTHR11070:SF48; PTHR11070:SF48; 2.
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..1216
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379333"
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