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Database: UniProt
Entry: A0AL19
LinkDB: A0AL19
Original site: A0AL19 
ID   ADDB_LISW6              Reviewed;        1157 AA.
AC   A0AL19;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   18-JUL-2018, entry version 82.
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};
GN   OrderedLocusNames=lwe2283;
OS   Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 /
OS   SLCC5334).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=386043;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35897 / DSM 20650 / SLCC5334;
RX   PubMed=16936040; DOI=10.1128/JB.00758-06;
RA   Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R.,
RA   Chatterjee S.S., Domann E., Kaerst U., Goesmann A., Bekel T.,
RA   Bartels D., Kaiser O., Meyer F., Puehler A., Weisshaar B., Wehland J.,
RA   Liang C., Dandekar T., Lampidis R., Kreft J., Goebel W.,
RA   Chakraborty T.;
RT   "Whole-genome sequence of Listeria welshimeri reveals common steps in
RT   genome reduction with Listeria innocua as compared to Listeria
RT   monocytogenes.";
RL   J. Bacteriol. 188:7405-7415(2006).
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; AM263198; CAK21701.1; -; Genomic_DNA.
DR   RefSeq; WP_011703032.1; NC_008555.1.
DR   ProteinModelPortal; A0AL19; -.
DR   SMR; A0AL19; -.
DR   STRING; 386043.lwe2283; -.
DR   PRIDE; A0AL19; -.
DR   EnsemblBacteria; CAK21701; CAK21701; lwe2283.
DR   KEGG; lwe:lwe2283; -.
DR   eggNOG; ENOG4105C5N; Bacteria.
DR   eggNOG; COG3857; LUCA.
DR   HOGENOM; HOG000285805; -.
DR   KO; K16899; -.
DR   OMA; HFASHGL; -.
DR   OrthoDB; POG091H01PC; -.
DR   BioCyc; LWEL386043:G1GJF-2349-MONOMER; -.
DR   Proteomes; UP000000779; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:InterPro.
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; 1.
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.
FT   CHAIN         1   1157       ATP-dependent helicase/deoxyribonuclease
FT                                subunit B.
FT                                /FTId=PRO_0000379198.
FT   DOMAIN        1    277       UvrD-like helicase ATP-binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01452}.
FT   DOMAIN      272    578       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       794    794       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      1118   1118       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01452}.
FT   METAL      1124   1124       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01452}.
SQ   SEQUENCE   1157 AA;  132447 MW;  89B48C197EAB1C82 CRC64;
     MTLQIIAGKS GTGKTTHLMD EVGKKIKKTS KTYIFIVPDQ MTFQMETSFL NKESLSGMLG
     TQIFSFSRLA WKILQETGGL SKTFLSQTGI EMVIRKAALD QKDKLKIFSK ATSRKGFYSE
     LAKLFKEMKQ EEVSVADLEN SAINMSKSVT NKIHDISLIY QKYEELLAGK FLENEDYLRL
     LADKIIESDY LNQTEIIIDG FTSFSKQELT VIEKLMEKCD KVTVSLTLNV PEIQKGLEEY
     NMFKQSTEAY FALLEMAKLN KISVESDKLF LENKRAKSDS LAFLADVWGN NKFVTFEEKP
     QDLAIHQANN RRAEIEGIAR EIRQLTLKGY RYQDMAILTR NISDYDVLCE TVMESFDIPI
     FIDKKRAMAK HPFIEFIRSS IDAILFNWKY EPIFQAVKTE FFFDVSENTS IMRRKADILE
     NYVLENGIQN KWKWEKEGDW IYRKIRGLST NLLPQTDEEL ETQAIINEMR NLIVEPLSIL
     ENNLAKARTG TEFAMALYHF LEQVKAVEHL ESWRQTAEEN GYLELAREHE QAWSSVSELL
     DEFVEVLGEE SLDINSFAEI VATGLDALEF SLLPPSLDQI VLSDMENAKL LDMKVIFAIG
     MNDGIMPLRQ KDKGILSDQD RDSLRAENSN LKPSAKNNIG EEDLLAYKII SLPSDKLFLS
     YPAADEEGKV LSESNYLRKI KGQFKKLNEE VYLTDPSLLS DEEQSSYIRS KQATLGLLTS
     QLQMYKRGYP LSNVWWDAYN GYFEDTKESK VAKQVLSSLY YENKTKALHE TTAKNLFGEN
     IHASVSRMEK FFSCEFQHFA QYGLKLEERA HFKLQAVDMG EIFHGAMEWI SAELKRNNQD
     WGNLTEEECR QMAKLAMTFL APKIQHEILL SSKRMEYIQY KLLQIITRAT TVLNEQAKSS
     AFRPIGLEVD FGLKGDIPSL KIPLKSESEL LLQGRIDRID VAEQDDRTFL RIIDYKSSSH
     DLALTEVYYG LALQMLTYLD IVVTNAQKMI GKTAEPAGVL YFHMHNQFVQ ADKELSDEAI
     AKELQKSSKM KGLILSDPVA VSLMDTSLEK GKSSNIIPAE IKQNGDLSAR SRTATKEEFD
     KMRHFVRHKY QEAGNKILDG AVSINPYKLK ERTPCQFCGF RSFCGFDPSL TSNQYRHLTN
     EKAENILTKM DIEGGTQ
//
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