GenomeNet

Database: UniProt
Entry: Q3K1I4
LinkDB: Q3K1I4
Original site: Q3K1I4 
ID   ADDA_STRA1              Reviewed;        1207 AA.
AC   Q3K1I4;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   05-DEC-2018, entry version 84.
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=SAK_0997;
OS   Streptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC
OS   SS700).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=205921;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27591 / A909 / CDC SS700;
RX   PubMed=16172379; DOI=10.1073/pnas.0506758102;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Donati C., Medini D.,
RA   Ward N.L., Angiuoli S.V., Crabtree J., Jones A.L., Durkin A.S.,
RA   DeBoy R.T., Davidsen T.M., Mora M., Scarselli M., Margarit y Ros I.,
RA   Peterson J.D., Hauser C.R., Sundaram J.P., Nelson W.C., Madupu R.,
RA   Brinkac L.M., Dodson R.J., Rosovitz M.J., Sullivan S.A.,
RA   Daugherty S.C., Haft D.H., Selengut J., Gwinn M.L., Zhou L., Zafar N.,
RA   Khouri H., Radune D., Dimitrov G., Watkins K., O'Connor K.J.,
RA   Smith S., Utterback T.R., White O., Rubens C.E., Grandi G.,
RA   Madoff L.C., Kasper D.L., Telford J.L., Wessels M.R., Rappuoli R.,
RA   Fraser C.M.;
RT   "Genome analysis of multiple pathogenic isolates of Streptococcus
RT   agalactiae: implications for the microbial 'pan-genome'.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13950-13955(2005).
CC   -!- FUNCTION: The heterodimer acts as both an ATP-dependent DNA
CC       helicase and an ATP-dependent, dual-direction single-stranded
CC       exonuclease. Recognizes the chi site generating a DNA molecule
CC       suitable for the initiation of homologous recombination. The AddA
CC       nuclease domain is required for chi fragment generation; this
CC       subunit has the helicase and 3' -> 5' nuclease activities.
CC       {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}.
DR   EMBL; CP000114; ABA45488.1; -; Genomic_DNA.
DR   RefSeq; WP_000143231.1; NC_007432.1.
DR   SMR; Q3K1I4; -.
DR   EnsemblBacteria; ABA45488; ABA45488; SAK_0997.
DR   KEGG; sak:SAK_0997; -.
DR   HOGENOM; HOG000285114; -.
DR   KO; K16898; -.
DR   OMA; KQSIYRW; -.
DR   BioCyc; SAGA205921:G1G54-1027-MONOMER; -.
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:0004003; F:ATP-dependent 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; 3.90.320.10; -; 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; IPR011604; Exonuc_phg/RecB_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038726; PDDEXK_AddAB-type.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   InterPro; IPR034739; UvrD/AddA_N.
DR   PANTHER; PTHR11070; PTHR11070; 1.
DR   PANTHER; PTHR11070:SF14; PTHR11070:SF14; 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;
KW   Helicase; Hydrolase; Nuclease; Nucleotide-binding.
FT   CHAIN         1   1207       ATP-dependent helicase/nuclease subunit
FT                                A.
FT                                /FTId=PRO_0000379326.
FT   DOMAIN       26    482       UvrD-like helicase ATP-binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01451}.
FT   DOMAIN      508    794       UvrD-like helicase C-terminal.
FT                                {ECO:0000255|HAMAP-Rule:MF_01451}.
FT   NP_BIND      47     54       ATP. {ECO:0000255|HAMAP-Rule:MF_01451}.
SQ   SEQUENCE   1207 AA;  139446 MW;  8F7247D5DFC85196 CRC64;
     MTFKPFLNPE DIAVIQTEEK NSDKKQKRTP EQIEAIYTFG NNVLVSASAG SGKTFVMVER
     ILDKLLRGVP IDSLFISTFT VKAAGELKER LEKKINESLK SAESDDLKQF LTQQLVGIQT
     ADIGTMDAFT QKIVNQYGYT LGISPIFRIL QDKNEQDVIK NEVYADLFSD YMTGKNAASF
     IKLVKNFSGN RKDSKAFREM VYKVYAFSQS TDNPKRWMQT VFLKGAQTYT DFEAIPDQEV
     SSLLNVMQTT ANQLRDLTDQ EDYKQLTAKG VPTANYKKHL KIIENLVHWS QDFNLLYGKK
     GLTNLARDIT NVIPSGNDVT VAGVKYPIFK QLHNRIVGLK HLEVIFKYQG ESLFLLELLQ
     SFVLDFSEQY LQEKIQENAF EFSDIAHFAI QILEENHDIR QLYQDKYHEV MVDEYQDNNH
     TQERMLELLS NGHNRFMVGD IKQSIYRFRQ ADPQIFNDKY KAYQDNPSQG KLIILKENFR
     SQSEVLDSTN SVFTHLMDEE VGDILYDESH QLKAGSPRQQ ERHPNNKTQV LLLDTDEDDI
     DDSDSQQYDI SPAEAKLVAK EIIRLHKEEN VPFQDITLLV SSRTRNDGIL QTFDRYGIPL
     VTDGGEQNYL KSVEVMVMLD TLRSIDNPLN DYALVALLRS PMFGFNEDDL TRIAIQDVKM
     AFYHKVKLSY HKEGHHSDLI TPELSSKIDH FMKTFQTWRD FAKWHSLYDL IWKIYNDRFY
     YDYVGALPKA EQRQANLYAL ALRANQFEKT GFKGLSRFIR MIDKVLENEN DLADVEVALP
     QNAVNLMTIH KSKGLEFKYV FILNIDKKFS MVDITSPLIL SRNQGIGIKY VADMRHELEE
     EILPAVKVSM ETLPYQLNKR ELRLATLSEQ MRLLYVAMTR AEKKLYLVGK ASQTKWADHY
     DLVSENNHLP LASRETFVTF QDWLLAVHET YKKQELFYDI NFVSLEELTD HHIGMVNPSL
     PFNPDNKVEN RQSEDIVRAI SVLESVEQIN QTYKAAIELP TVRTPSQVKK FYEPILDIEG
     VDVMETITKT SVDFKLPDFS TSKKQDPAAL GSAVHELMQR IEMSSHVKME DIQKALTEVN
     AETSVKAAIQ IEKINYFFQE TSLGKYIQEE VEHLHREAPF AMLKEDPESG EKFVVRGIID
     GYLLLENRII LFDYKTDKFV NPLELKERYQ GQMALYAEAL KKSYEIEKID KYLILLGGKQ
     LEVVKMD
//
DBGET integrated database retrieval system