ADDA_STRP2
ID ADDA_STRP2 Reviewed; 1216 AA.
AC Q04KF8;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=SPD_1016;
OS Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=373153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D39 / NCTC 7466;
RX PubMed=17041037; DOI=10.1128/jb.01148-06;
RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT pneumoniae and comparison with that of unencapsulated laboratory strain
RT R6.";
RL J. Bacteriol. 189:38-51(2007).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000410; ABJ53740.1; -; Genomic_DNA.
DR RefSeq; WP_000767212.1; NC_008533.2.
DR AlphaFoldDB; Q04KF8; -.
DR SMR; Q04KF8; -.
DR STRING; 373153.SPD_1016; -.
DR EnsemblBacteria; ABJ53740; ABJ53740; SPD_1016.
DR GeneID; 60233267; -.
DR KEGG; spd:SPD_1016; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR OrthoDB; 137860at2; -.
DR BioCyc; SPNE373153:G1G6V-1104-MON; -.
DR Proteomes; UP000001452; 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_0000379339"
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
