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ADDB_BACMK
ID   ADDB_BACMK              Reviewed;        1171 AA.
AC   A9VJ01;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=BcerKBAB4_1040;
OS   Bacillus mycoides (strain KBAB4) (Bacillus weihenstephanensis).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBAB4;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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 AddB nuclease domain is not
CC       required for chi fragment generation; this subunit has 5' -> 3'
CC       nuclease activity. {ECO:0000255|HAMAP-Rule:MF_01452}.
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_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 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01452}.
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DR   EMBL; CP000903; ABY42290.1; -; Genomic_DNA.
DR   RefSeq; WP_012260537.1; NC_010184.1.
DR   AlphaFoldDB; A9VJ01; -.
DR   SMR; A9VJ01; -.
DR   STRING; 315730.BcerKBAB4_1040; -.
DR   EnsemblBacteria; ABY42290; ABY42290; BcerKBAB4_1040.
DR   KEGG; bwe:BcerKBAB4_1040; -.
DR   eggNOG; COG3857; Bacteria.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OMA; DRLENYV; -.
DR   Proteomes; UP000002154; 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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
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   Gene3D; 3.40.50.300; -; 4.
DR   Gene3D; 3.90.320.10; -; 1.
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; IPR011604; PDDEXK-like_dom_sf.
DR   InterPro; IPR038726; PDDEXK_AddAB-type.
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; DNA damage; DNA repair; Exonuclease; Hydrolase; Iron;
KW   Iron-sulfur; Metal-binding; Nuclease; Nucleotide-binding.
FT   CHAIN           1..1171
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379166"
FT   DOMAIN          1..301
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   DOMAIN          281..587
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         8..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         805
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1129
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1132
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1138
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ   SEQUENCE   1171 AA;  134314 MW;  4BD5C19CFFA15DD7 CRC64;
     MSLRFVIGRA GSGKSTLCLH EVQEELKQRP RGKTILYLVP EQMTFQTQQA LIGSEDVRGS
     IRAQVFSFSR LAWKVLQEVG GASRLHIDEA GVHMLLRKIV ESRKDGLSVF QKAAEQNGFF
     EHLGSMIAEF KRYNVTPSNV YEMWQQLDTH SSSAEQKLLA NKVYDLQLLY DDFERALIGK
     YLDSEDYLQL LIEKLSDSEY VKGAEIYIDG FHSFSPQELE IVRGLMRLGT RVTITLTIDE
     KTLAQPVNEL DLFYETTLTY ERIKQVAREE KIEVEKTIPL MKQPRFHSQA LAHLEMHYEA
     RPNEKFHGEA SVTISTAANL RAEVEGVARE IRRLVATEDY RYRDIAVLLR NGESYYDVMR
     TLFTDYNIPH FIDEKRPMSH HPLVECIRSA LEIISGNWRY DAVFRCVKTE LLYPLDVRKE
     AMREEMDEFE NYCLAYGVQG KRWTSEDPWM YRRYRSLDDA SEMITDSERE MEEKINRLRD
     VVRTPVIRMQ KRLKRAGTVM QMCEAVYLFL EELDVPKKLE ALRIRAEESG DFLFATDHEQ
     VWEEVMSLLD TFVEMLGEEK MSLSMFTDVM TTGLEALQFA NIPPSLDQVL VANIDHSRLS
     DIKATFIIGV NEGVIPAAPM DEGMLSDEER NVLTAAGIEL APTTRQTLLE EQFVMYQMVT
     RASEKLYISC PLADEEGKTL LASSFIKKIK RMFPDVKESF ITNDVNDLSR SEQLSYVATP
     EVTLSYVMQQ LQTWKRYGFE GNLDFWWDVY NFYVTSDEWK QKSSRVLSSL FYRNRAQKLS
     TDVSRDLYGD TIKGSVSRME LFNRCAYAHF AQHGLSLRER DIFKLDAPDI GELFHAALKR
     IADKLLRENR TWADLSIKEC EHLSALVIEE IAPLLQRQIL LSSNRHFYLK QKLQQIIFRT
     SLILREHAKS SGFVPVDLEV PFGMGGTGSL PPMEFALPNG VKMEVVGRID RVDKAEDESG
     TFLRIIDYKS SSKALDLTEV YYGLALQMLT YLDVVTSNAH TWMKKGSTAS PAGVLYFHIH
     NPIVEMKGDA SEEEIEKEIL KKFKMKGLVL GDADVVRLMD NKLSTGSSDI ISAGLKKDGS
     FSARSSIASE QEFNVLQKYV HHSFENIGKD ITEGVIDIAP YKKGNKAACT FCNFKSVCQF
     DESLEDNQFR TLKDMKDSEA MEKIREEVGG E
 
 
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