ADDA_STREM
ID ADDA_STREM Reviewed; 1214 AA.
AC B4U2H1;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
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}; OrderedLocusNames=Sez_0829;
OS Streptococcus equi subsp. zooepidemicus (strain MGCS10565).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=552526;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGCS10565;
RX PubMed=18716664; DOI=10.1371/journal.pone.0003026;
RA Beres S.B., Sesso R., Pinto S.W.L., Hoe N.P., Porcella S.F., Deleo F.R.,
RA Musser J.M.;
RT "Genome sequence of a lancefield group C Streptococcus zooepidemicus strain
RT causing epidemic nephritis: new information about an old disease.";
RL PLoS ONE 3:E3026-E3026(2008).
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; CP001129; ACG62188.1; -; Genomic_DNA.
DR RefSeq; WP_012515462.1; NC_011134.1.
DR AlphaFoldDB; B4U2H1; -.
DR SMR; B4U2H1; -.
DR EnsemblBacteria; ACG62188; ACG62188; Sez_0829.
DR KEGG; sez:Sez_0829; -.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000001873; 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..1214
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379330"
FT DOMAIN 27..483
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 512..800
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT BINDING 48..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1214 AA; 138506 MW; 59B73925401E2221 CRC64;
MRIDEGFLTP EAIARLQQEE ALSDKRHKRT AQQIEAIYSS GQNILVSASA GSGKTFVMVE
RILDKILRGI SVDRLFISTF TVKAATELIE RIEKKLHTAI AETQDYQLKA YLNDQLQALS
QADIGTMDAF AQKLVHQHGY VLGISPHFRI IQDKAEQDIL KREVFRQVFE DYMSQTDNKA
FIQLVQNFSG RRKDSSAFRE IVDSIYAFSQ STANPSSWLA EVFLRGAKTY TSFADIPDQV
VDALLACMQD TADQLRDLTD MEGYAQTTKA GKLTAKYTKH LKMIDNLYEW ASHFDSLYGK
ERLGQLAQEL TALLPSGADI TVAGHKYPIF KSLQEQLVGF RHLETILAYQ QESLPLLEVL
QAFVISFSEA YLAAKMQENA FEFSDIAHFA IEILQQAPDI RQAYQGHYHE VMVDEYQDNN
HMQERLLELL SNGHNRFMVG DIKQSIYRFR QADPQIFNQK FKDYQSNPEH GKLILLKENF
RSQSEVLNVT NAVFSRLMDE SLGEITYDDK HQLVAGSEAQ KQLHPENRAQ LLLYNTDQAQ
EGTEEASTND GISAGEVTLV AKEIIRLYNE EKVAFEDITL LVSSRTRNDT IFQVFNQYGI
PLVADGGQEN YLKSVEVMVM LDTLRSINNP LNDYALVALM RSPMFSFDED QLARISLQSS
SQDQPQAFYD KLSNSLRGQG EHPGLIGQEL MTKLVDFDRT LRDWRQFAKL HSLYELIWKI
FNDRFYFDFV ASQPKAEQAQ ANLYALAIRA DQFEQSGYKG LSRFIGMIDK VLETQNDLAD
VEVERPKHAV NLMTIHKSKG LEFHYVFILN FDKRFAMADL QAPIILNRDE GIGIKYVANV
KELLRDEKLA SLKVTMETLP YQLNKQQLRL ATLSEQMRLL YVAMTRAEKK VYLVGKASKE
KIQAKTADNS SEGRLALASR ERLLSFQDWL LAITATFSKE DLFIDVRFVD DSDLTAEAVG
QLRSSGLLQA DDLKDNRQTE DIARALDMLD KVSKLNASYQ AAIELPTVRT PSQLKTLYEP
LMDTDGVDII DQPYHRPKSF ELPDFSKKKA VEPSQVGSSL HELMQRIPMS DQITAGDIEQ
ALQLVSADAE VKARLDIKKV TAFFATTELG KLLQEHHQRL YREAPFAILK KDSLSQEQYV
VRGIIDGYLL FEDRIVLFDY KTDRYQQSAE LKQRYQQQMD LYAEALSQSY GIARVEKYLV
LMGGSQLEVV RLDE
