ADDA_STRPS
ID ADDA_STRPS Reviewed; 1216 AA.
AC B2IPX3;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=SPCG_1145;
OS Streptococcus pneumoniae (strain CGSP14).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=516950;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGSP14;
RX PubMed=19361343; DOI=10.1186/1471-2164-10-158;
RA Ding F., Tang P., Hsu M.-H., Cui P., Hu S., Yu J., Chiu C.-H.;
RT "Genome evolution driven by host adaptations results in a more virulent and
RT antimicrobial-resistant Streptococcus pneumoniae serotype 14.";
RL BMC Genomics 10:158-158(2009).
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; CP001033; ACB90397.1; -; Genomic_DNA.
DR RefSeq; WP_000767235.1; NC_010582.1.
DR AlphaFoldDB; B2IPX3; -.
DR SMR; B2IPX3; -.
DR EnsemblBacteria; ACB90397; ACB90397; SPCG_1145.
DR KEGG; spw:SPCG_1145; -.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000001682; 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_0000379336"
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; 140272 MW; 41097B1CDA6CF0BB CRC64;
MKLIPFLSEE EIQKLQEAEA NSSKEQKKTA EQIEAIYTSG QNILVSASAG SGKTFVMAER
ILDQLARGVE ISQLFISTFT VKAATELKER LEKKISKKIQ ETDDVDLKQH LGRQLADLPN
AAIGTMDSFT QKFLGKHGYL LDIAPNFRIL QNQSEQLLLE NEVFHEVFEA HYQGKQKETF
SHLLKNFAGR GKDERGLRQQ VYKIYDFLQS TSNPQKWLSK SFLKGFEKAD FTSEKEKLTE
QIKQALWDLE SFFRYHLDND AKEFAKAAYL ENVQLILDEI DSLNQESDSQ AYQAVLARVV
AISKEKNGRA LTNASRKADL KPLADTYNEE RKTQFAKLGQ LSDQIAILDY QERYHGDTWK
LAKTFQSFMS DFVEAYRQRK RQENAFEFAD ISHYTIEILE NFPQVRESYQ ERFHEVMVDE
YQDTNHIQER MLELLSNGHN RFMVGDIKQS IYRFRQADPQ IFNEKFQRYA QNPQEGKLIL
LKENFRSSSE VLSATNDVFE RLMDQEVGEI NYDNKHQLVF ANTKLTPNPD NKAEFLLYDK
DDTGEEEESQ TETKLTGEMR LVIKEILKLH QEKGVAFKEI ALLTSSRNRN DQILLALSEY
GIPVKTDGEQ NNYLQSLEVQ VMLDTLRVIH NPLQDYALVA LMKSPMFGFD EDELARLSLQ
KAEDKAHENL YEKLVNAQKK ASSQKGLIHT ALAEKLKQFM DILASWRLYA KPHSLYDLIW
KIYNDRFYYD YVGALPNGPA RQANLYALAL RADQFEKSNF KGLSRFIRMI DQVLEAQHDL
ASVAVAPPKD AVELMTIHKS KGLEFPYVFI LNMDQDFNKQ DSMSEVILSR QNGLGVKYIA
KMETGAVEDH YPKTIKLSIP SLTYRQNEEE LQLASYSEQM RLLYVAMTRA EKKLYLVGKG
SREKLEAKQY PAAKNGKLNS NTRLQARNFQ DWLWAISKVF TKDKLNFSYR FIGEDQLTRE
AIGELETKSP LRDSSQADNR QSDTIKEALE MLKEVEVYNT LHRAAIELPS VQTPSQIKKF
YEPVMDMEGV EIAGQGQSVG KKISFDLPDF STKEKVTGAE IGSATHELMQ RIDLSQQLTL
ASLTETLKQV QTSQAVRDKI NLDKILAFFD TVLGQEILAN TDHLYREQPF SMLKRDQKSQ
EDFVVRGILD GYLLYENKIV LFDYKTDRYD EPSQLVDRYR GQLALYEEAL SRAYSIKNIE
KYLILLGKDE VQVVKV
