ID ADDA_STRP4 Reviewed; 1216 AA.
AC B5E4P5;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 27-MAR-2024, entry version 86.
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=SPG_1051;
OS Streptococcus pneumoniae serotype 19F (strain G54).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=512566;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G54;
RX PubMed=11442348; DOI=10.1089/10766290152044995;
RA Dopazo J., Mendoza A., Herrero J., Caldara F., Humbert Y., Friedli L.,
RA Guerrier M., Grand-Schenk E., Gandin C., de Francesco M., Polissi A.,
RA Buell G., Feger G., Garcia E., Peitsch M., Garcia-Bustos J.F.;
RT "Annotated draft genomic sequence from a Streptococcus pneumoniae type 19F
RT clinical isolate.";
RL Microb. Drug Resist. 7:99-125(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G54;
RA Mulas L., Trappetti C., Hakenbeck R., Iannelli F., Pozzi G., Davidsen T.M.,
RA Tettelin H., Oggioni M.;
RT "Pneumococcal beta glucoside metabolism investigated by whole genome
RT comparison.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001015; ACF56108.1; -; Genomic_DNA.
DR RefSeq; WP_000767263.1; NC_011072.1.
DR AlphaFoldDB; B5E4P5; -.
DR SMR; B5E4P5; -.
DR KEGG; spx:SPG_1051; -.
DR HOGENOM; CLU_001114_3_1_9; -.
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:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
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.
FT CHAIN 1..1216
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379338"
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; 140300 MW; 415820C220FE2DAC CRC64;
MKLIPFLSEE EIQKLQEAEA NSSKEQKKTA EQIEAIYTSG QNILVSASAG SGKTFVMVER
ILDQLARGVE ISQLFISTFT VKAATELKER LEKKISKKIQ ETDDVDLKQH LGRQLADLPN
AAIGTMDSFT QKFLGKHGYL LDIAPNFRIL QNQSEQLLLE NEVFHEVFEA HYQGKQKESF
SHLLKNFAGR GKDERGLRQQ VYKIYDFLQS TSNPQKWLSE SFLKGFEKAD FTSEKEKLTE
QIKQALWDLE SFFRYHLDND AKEFAKAAYL ENVQLILDEI GSLNQEFDSQ AYQAVLARVV
AISKEKNGRA LTNASRKADL KPLADAYNEE RKTQFTKLGQ LSDQIAILDY QERYHGDTWK
LAKTFQSFMS DFVEAYRQRK RQENAFEFAD ISHYTIEILE NFPQVRESYQ ERFHEVMVDE
YQDINHIQER MLELLSNGHN RFMVGDIKQS IYRFRQADPQ IFNEKFQRYA QNPQEGKLIL
LKENFRSSSE VLSATNDVFE RLMDQEVGEI NYDNMHQLVF 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
SREKLESKEY PAAKNGKLNS NTRLQARNFQ DWLWAISKVF TKDKLNFSYR FIGEDQLTRE
AIGELETKSP LQDSSQADNR QSDTIKEALE MLKEVEVYNT LHRAAIELPS VQTPSQIKKF
YEPVMDMEGV EIAGQGQSVG KKISFDLPDF STKEKVTGAE IGSATHELMQ RIDLSQQLTL
ASLTETLKQV QTSQAVRDKI NLDKILAFFD TALGQEIFAN TDHLYREQPF SMLKRDQKSQ
EDFVVRGILD GYLLYENKIV LFDYKTDRYD EPSQLVDRYR GQLALYEEAL SRAYSIENIE
KYLILLGKDE VQVVKV
//
