ADDA_STRPI
ID ADDA_STRPI Reviewed; 1216 AA.
AC B1IBR6;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
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}; Synonyms=rexA;
GN OrderedLocusNames=SPH_1226;
OS Streptococcus pneumoniae (strain Hungary19A-6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=487214;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hungary19A-6;
RX PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA Rappuoli R., Moxon E.R., Masignani V.;
RT "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT closely related species.";
RL Genome Biol. 11:R107.1-R107.19(2010).
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; CP000936; ACA37039.1; -; Genomic_DNA.
DR RefSeq; WP_000767219.1; NC_010380.1.
DR AlphaFoldDB; B1IBR6; -.
DR SMR; B1IBR6; -.
DR EnsemblBacteria; ACA37039; ACA37039; SPH_1226.
DR GeneID; 66806235; -.
DR KEGG; spv:SPH_1226; -.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000002163; 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_0000379337"
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; 140231 MW; 8865E7AC483F3197 CRC64;
MKLIPFLSEE EIQKLQEAEA NSSKEQKKTA EQIEAIYTSG QNILVSASAG SGKTFVMAER
ILDQLARGVE ISQLFISTFT VKAANELKER LEKKISKKIQ ETDDVDLKQH LGRQLADLPN
AAIGTMDSFT QKFLGKHGYL LDIAPNFRIL QNQSEQLLLE NEVFHEVFEA HYQGKQKETF
SHLLKNFAGR GKDERGLRQQ VYKIYDFLQS TSNPQKWLSD SFLKGFEKAD FTSEKEKLTE
QIKQALWDLE SFFRYHLDND AKEFAKAAYL ENVQLILDEI GSLNQESDSQ AYQAVLAHVV
AISKEKNGRA LTNASRKADL KPLADAYNEE RKTQFAKLGQ LSDQITILDY QERYHGDTWK
LAKTFQSFMS DFVEAYRQRK RQENAFEFAD ISHYTIEILE NFPQVRESYQ ERFHEVMVDE
YQDTNHIQER MLELLSNGHN RFMVGDIKQS IYRFRQADPQ IFNEKFQRYA QNPQEGKLIL
LKENFRSSSE VLSATNDVFE RLMDQEVGEI NYDNKHQLVF ANTKLTPNPD NKAEFLLYDK
DDTGEEEESQ TETKLTGEMR LVIKEILKLH QEKGVAFKEI ALLTSSRSRN DQILLALSEY
GIPVKTDGEQ NNYLQSLEVQ VMLDTLRVIH NPLQDYALVA LMKSPMFGFD EDELARLSLQ
KAEDKVHENL YEKLVNAQKM ASSQKGLIHT ALAEKLKQFM DILASWRLYA KTHSLYDLIW
KIYNDRFYYD YVGALPNGPA RQANLYALAL RADQFEKSNF KGLPRFIRMI DQVLEAQHDL
ASVVVAPPKD 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
