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Database: UniProt
Entry: Q5HQJ5
LinkDB: Q5HQJ5
Original site: Q5HQJ5 
ID   ADDB_STAEQ              Reviewed;        1159 AA.
AC   Q5HQJ5;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   10-OCT-2018, entry version 94.
DE   RecName: Full=ATP-dependent helicase/deoxyribonuclease subunit B {ECO:0000255|HAMAP-Rule:MF_01452};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01452};
DE            EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01452};
DE   AltName: Full=ATP-dependent helicase/nuclease AddB {ECO:0000255|HAMAP-Rule:MF_01452};
GN   Name=addB {ECO:0000255|HAMAP-Rule:MF_01452}; Synonyms=rexB;
GN   OrderedLocusNames=SERP0554;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T.,
RA   Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J.,
RA   Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S.,
RA   Haft D.H., Vamathevan J.J., Khouri H., Utterback T.R., Lee C.,
RA   Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H.,
RA   Hance I.R., Nelson K.E., Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete
RT   genome analysis of an early methicillin-resistant Staphylococcus
RT   aureus strain and a biofilm-producing methicillin-resistant
RT   Staphylococcus epidermidis strain.";
RL   J. Bacteriol. 187:2426-2438(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 AddB
CC       nuclease domain is not required for chi fragment generation; this
CC       subunit has 5' -> 3' nuclease activity. {ECO:0000255|HAMAP-
CC       Rule:MF_01452}.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_01452}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01452};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01452};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01452};
CC   -!- SUBUNIT: Heterodimer of AddA and AddB. {ECO:0000255|HAMAP-
CC       Rule:MF_01452}.
CC   -!- SIMILARITY: Belongs to the helicase family. AddB/RexB type 1
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01452}.
DR   EMBL; CP000029; AAW53933.1; -; Genomic_DNA.
DR   RefSeq; WP_001831905.1; NC_002976.3.
DR   ProteinModelPortal; Q5HQJ5; -.
DR   SMR; Q5HQJ5; -.
DR   STRING; 176279.SERP0554; -.
DR   PRIDE; Q5HQJ5; -.
DR   EnsemblBacteria; AAW53933; AAW53933; SERP0554.
DR   KEGG; ser:SERP0554; -.
DR   eggNOG; ENOG4105C5N; Bacteria.
DR   eggNOG; COG3857; LUCA.
DR   HOGENOM; HOG000033809; -.
DR   KO; K16899; -.
DR   OMA; HFASHGL; -.
DR   Proteomes; UP000000531; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0008409; F:5'-3' 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:InterPro.
DR   GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01452; AddB_type1; 1.
DR   InterPro; IPR014140; DNA_helicase_suAddB.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038726; PDDEXK_AddAB-type.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070; PTHR11070; 1.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR02773; addB_Gpos; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; ATP-binding; Complete proteome; DNA damage; DNA repair;
KW   Exonuclease; Hydrolase; Iron; Iron-sulfur; Metal-binding; Nuclease;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN         1   1159       ATP-dependent helicase/deoxyribonuclease
FT                                subunit B.
FT                                /FTId=PRO_0000379220.
FT   DOMAIN        1    275       UvrD-like helicase ATP-binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01452}.
FT   DOMAIN      269    583       UvrD-like helicase C-terminal.
FT                                {ECO:0000255|HAMAP-Rule:MF_01452}.
FT   NP_BIND       8     15       ATP. {ECO:0000255|HAMAP-Rule:MF_01452}.
FT   METAL       784    784       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01452}.
FT   METAL      1112   1112       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01452}.
FT   METAL      1115   1115       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01452}.
FT   METAL      1121   1121       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01452}.
SQ   SEQUENCE   1159 AA;  134920 MW;  251115B7A1C9EAA3 CRC64;
     MEFNTYIGRA GTGKSTAMLN QIKNKMKQDP LGDPIVLIAP TQSTFQLEQA FVNDSELHGS
     LRTEVLHFER LSHRVFQEVG GLTEQRLSKA ALEMMIFHIV QQHESDLKLY GSQAQYYGLS
     EKLAEQIQDF KKYNVTPEHL NQLIENHSIQ TRTKHKLEDI SLIYKQLESR MNGEFITTED
     SLQQFIEILS QSQWIKKAEV FIDGFHNFST LEYRIIEALV QHAKQVTVLL TTDGSHHPFS
     LFRKPSEVLS HLEDIANRLN INLNKTYFNT FYRYNNDDLK NLENGFDALQ FTPKHHQNHV
     KIFESSSMRE EINEVARRIL KDVREADYKF RDIAILYRDE SYAYLFESIL PSYDIPFNID
     TKKSMTHHPI MEMLRSLLEV IRSNWHINAM LRLFKTNVLT SQFKRSSYLI DLLENFVLER
     GIYGKRWLDE DIFSIDQFSR MGRKSHQLTE GHQALYKEVI KLKKNVINKV LYFEQAMNEA
     HTVKDYATSF YESLEYFELP SQLMTQRDEL ELAGLTEKAE EIDQVWNGLI QILDDLVTVF
     DDQEMTLQQF LDVFDIGLEQ LEFVMIPQTL DQVSIGTMDL AKVDNKKHIY MVGMNDGILP
     QTVSSSSLIT DEEKKYVEDN AHVELSPTSD ILQMDEAFVC YIAMTRSQQS VTFSYSLMGN
     SGDEKEISPF LTQIKELFYD LEITNLQDLH KAQPLLMMQH SHQTKIQLFE YLRGWLDHED
     IDYRWLDAYL AIRDDDQLNQ GLDYLTTSLT YDNETVQLNE ILSQQLYGKT INASVSRFEG
     YQQCPFKHYA SHGLRLNERT KYELQNFDLG DIFHSVLKYI SDRIYGDFKN LDTKNIQSLT
     KEALELILPK VQFNLLNSSA YYKYLSKKIG SIVETTLKAL KYQGEYSKFV PQRFETGFRK
     SPKNKGELVA QPLITNQGIP INIRGQIDRI DTYTKGDHSY VNIIDYKSSE SSATLDLTKV
     YYGLQMQMMT YMDIVLQNKE RLGLTDIVKP GGLLYFHVHE PRIKFKSWAD IDEDQFQKDY
     IKNFKMSGLL NRDQEVLDAL DIRLEPKYNS DIVPIALTAK GAINQRSSKV ADENIIYQLI
     EHNKKNFIET ASHIMDGHTE VAPLKYKQVL PCQFCNYKSV CHVDGLIDSK RYRTVDESIK
     PLDLIQQLRN EGGERHDSN
//
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