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Database: UniProt
Entry: A8FBR0
LinkDB: A8FBR0
Original site: A8FBR0 
ID   ADDB_BACP2              Reviewed;        1169 AA.
AC   A8FBR0;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   25-APR-2018, entry version 71.
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=BPUM_0993;
OS   Bacillus pumilus (strain SAFR-032).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=315750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAFR-032;
RX   PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA   Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA   Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C.,
RA   Dinh H., Lee S., Nazareth L., Blyth P., Holder M., Buhay C.,
RA   Tirumalai M.R., Liu Y., Dasgupta I., Bokhetache L., Fujita M.,
RA   Karouia F., Eswara Moorthy P., Siefert J., Uzman A., Buzumbo P.,
RA   Verma A., Zwiya H., McWilliams B.D., Olowu A., Clinkenbeard K.D.,
RA   Newcombe D., Golebiewski L., Petrosino J.F., Nicholson W.L., Fox G.E.,
RA   Venkateswaran K., Highlander S.K., Weinstock G.M.;
RT   "Paradoxical DNA repair and peroxide resistance gene conservation in
RT   Bacillus pumilus SAFR-032.";
RL   PLoS ONE 2:E928-E928(2007).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABV61677.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; CP000813; ABV61677.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041815374.1; NC_009848.4.
DR   SMR; A8FBR0; -.
DR   STRING; 315750.BPUM_0993; -.
DR   PRIDE; A8FBR0; -.
DR   EnsemblBacteria; ABV61677; ABV61677; BPUM_0993.
DR   KEGG; bpu:BPUM_0993; -.
DR   eggNOG; COG3857; LUCA.
DR   HOGENOM; HOG000285805; -.
DR   KO; K16899; -.
DR   OrthoDB; POG091H01PC; -.
DR   BioCyc; BPUM315750:G1G9U-1053-MONOMER; -.
DR   Proteomes; UP000001355; 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: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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038726; PDDEXK_AddAB-type.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   Pfam; PF12705; PDDEXK_1; 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   1169       ATP-dependent helicase/deoxyribonuclease
FT                                subunit B.
FT                                /FTId=PRO_0000379163.
FT   DOMAIN        1    285       UvrD-like helicase ATP-binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01452}.
FT   DOMAIN      280    586       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       801    801       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}.
FT   METAL      1124   1124       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01452}.
FT   METAL      1130   1130       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01452}.
SQ   SEQUENCE   1169 AA;  134856 MW;  1F43DF6882C00EE8 CRC64;
     MEIQFLAGRS GSGKTTAILE EIKEQLRLDP LGPPIIFLVP DQMTFLMEYE LAKTSEAGGM
     IRAKVFSFTR LAWSILQQTG GANRQFVTST GIQMLLRKVI EEQKDKFKVF KKASDKPGFV
     EQIEKTMAEF KRYCMLPEEI EKISVESMLS EYTEERRAAE KLHDLHVLYQ QMEEHLQDEY
     VHSEDYLNLL AQQIPSAEEI KGAHIYIDGF YQFTPQQLLV IEQLLLHAAK VTAAFTVDQS
     YHDRQPNELD LFRMTGKTYF QLYQLAKECG ADISETIFER NHRHLYTPDL AYLEHQYEQR
     PVQPYQENTP HLTVSKSASK RAEIEGVARD ILDLVREKGL RLRDISVVAR HVDDYKDTLK
     EVFRDYDIPF FIDGNESMQY HPLIELIRSS LDVIKGNWRY EAVFRCVKTE FLFPLEITKN
     KAREQADQLE NYCIAYGVKG ERWTNGSRFH YRRFQSLDED FRQTDQEIEM EQMLNDVKEW
     ITPPLYQLQK RLKNAQKVRD MVEAVYVFLE EIQVPDKLEK ARLEAEEAGR LAEAMQHGQV
     WDAVIQLMDE FVDMLGDEEL SFPLFQQMID TGLASLKFAL IPPSLDQVFI GSMDLSRMYQ
     VKCMFIIGVN DGVIPARPSD ESVLSEDDRE WLKRAGAELA ETGKERLLDE QFLIYQALSS
     PSHHLYLSYA ASDAEGRSLL PSPLIKYCQE LMPNHQQALY VLDPELLEDD EQLKFVANEH
     VSLSYTISQL QQWLNQYPIS GVWWSVYNYL MTSPNRDVSK NIMSSLFFTN RAKPLKPNVT
     KELYGDHIQG SVSRMEKFNA CAFSHFASHG LKLKDRQFYK LEAPDIGQLF HSALKHISDT
     LVEQKKDWKN LTKEDCVTYS RHAIEQLAPR LQKEILLSSN RHAYIKEKLQ KILIRVSSIL
     SEHAKVSGFS PVGLELGFGG QGPLPPFTFQ LKNGCTMELV GRIDRVDKAE GSKGLFLRIV
     DYKSSEKGLD LAEVYYGLAL QMLTYLDLTI TYSKEWLGIE ATPAGILYFH IHDPFIQAPI
     PLAEDEIEQE IFKKFKMKGL LLEDVEAVKL MDQTLESGRS QVIQAGLKKD GSFRSDSAVL
     SEDHFHILTQ HVRRTFEEAG ERITNGEVAI NPYKLKDQTP CRFCSFKSIC QFDESIEDND
     FRVLTSEKDD VVIERIKKEG DQYANTKTE
//
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