ADDA_STAS1
ID ADDA_STAS1 Reviewed; 1219 AA.
AC Q49WA6;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=SSP1808;
OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS 20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=342451;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT pathogenesis of uncomplicated urinary tract infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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; AP008934; BAE18953.1; -; Genomic_DNA.
DR AlphaFoldDB; Q49WA6; -.
DR SMR; Q49WA6; -.
DR STRING; 342451.SSP1808; -.
DR PRIDE; Q49WA6; -.
DR EnsemblBacteria; BAE18953; BAE18953; SSP1808.
DR KEGG; ssp:SSP1808; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000006371; 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; 1.
DR PANTHER; PTHR11070:SF48; PTHR11070:SF48; 1.
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; Reference proteome.
FT CHAIN 1..1219
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379325"
FT DOMAIN 12..477
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 478..786
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT REGION 997..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1016
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1219 AA; 142417 MW; 2958748980BF55AA CRC64;
MMNAIPVKPT GTRWTDNQWK SIYAKGQDIL VAAAAGSGKT AVLVERIIQR IIRDEIDVDK
LLVVTFTNAS AREMKQRVDQ RIQEASIENP DNAHLKNQRV KIHQAQISTL HSFCLKLIQQ
HYDVLDIDPN FRTSSEAENI LLLEQTIDEV LERHYDILDP HFIDLTEQLS SDRNDDQLRN
TIKEMYYFSV ANPNPLNWLQ HLSTPYEDES QQETLFNLLN DLAMIFMNSA LEALNKSYDL
FMMLEEVDKQ VAVLDKERRF LAEAMEGGLL NTQKIAEHQF ESRFPAKNKK IKEANEMMID
AYDDGKKHYD DYKALVSKVQ EDYFSREAAD LKTDMQRLAP RVAYLAQVTA DVIEQFNQKK
RSRNLLDFSD YEHFALRILM DSNGNPSEIA DMYRKQFEEI LVDEYQDTNR VQEKIIACIK
RGDEADGNLF MVGDVKQSIY KFRQADPSLF IGKYNRFTLD GSEHGMRIDL SQNFRSREEV
LTTTNYLFKH MMDEAVGEIV YDDAAQLYYG APFDHKPHDV QLNMLIEDAS SDLNGSEQEA
EYIVQQVEKI MSQHEIYDIK TEQYRKPSYK DIVILERSYG QARKIQQAFK DHNIPFHVNS
KEGYFEQTEV QLILSFLRTI DNPLQDIYLV GLMRSVIYQF TEDELSNIRV FSPNDDYFYQ
SIKHYMANDV ANKKLVAKLA SFLEDIEQYQ DYSQSHPVYQ LIDKFYNDHY VIQYFSGIIG
GKGRRANLYG LFNKAVEFEN SSFRGLYQFI RFIDELIERG KDFGEENIVG PNDDVVRMMT
IHSSKGLEFP FVIYSGLSRK FRRDDLHRPV ILNQSYGLGM AYYDVESNLS YPSLSSVTYK
AIAEKEMVSE EMRLIYVALT RAKEQLFLIG RVKDEKTLSQ FEQVSVSESH LPVSYRITAQ
RPIDMIYPIL AKYQSSSLPN ELRFEQTIED VDQAMRPYVQ LNTDFYEDIA SETVTDVSEQ
RTVADIEMNH SKNEALQAQI HNQLSYEYPY QSAIEKPSKQ SVSELKRQHE TEQSDTNYDR
VRQYRIGSTS YERPAFLSRS KQRKANEIGT LMHTVMQHLP FNKDRLTEED VNRLVDHLIA
QHIIPEDAKQ DIRFDDIYNF IASDLYQLIA ESDEIYRELP FVVNQNEVDH NKHSEEDASI
IQGMIDLIFV KEGQYYFVDY KTDAFNRRRN MSDEEIGAQL RERYKVQMNH YRNTLETILK
TDVKGFLYFF KFGQLSIEG
