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ADDB_LYSSC
ID   ADDB_LYSSC              Reviewed;        1169 AA.
AC   B1HN89;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 89.
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}; OrderedLocusNames=Bsph_1198;
OS   Lysinibacillus sphaericus (strain C3-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=444177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C3-41;
RX   PubMed=18296527; DOI=10.1128/jb.01652-07;
RA   Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M.,
RA   Berry C., Yuan Z.;
RT   "Complete genome sequence of the mosquitocidal bacterium Bacillus
RT   sphaericus C3-41 and comparison with those of closely related Bacillus
RT   species.";
RL   J. Bacteriol. 190:2892-2902(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; CP000817; ACA38806.1; -; Genomic_DNA.
DR   RefSeq; WP_012292937.1; NC_010382.1.
DR   AlphaFoldDB; B1HN89; -.
DR   SMR; B1HN89; -.
DR   PRIDE; B1HN89; -.
DR   EnsemblBacteria; ACA38806; ACA38806; Bsph_1198.
DR   KEGG; lsp:Bsph_1198; -.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OMA; DRLENYV; -.
DR   Proteomes; UP000002164; 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   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; DNA damage; DNA repair; Exonuclease; Hydrolase; Iron;
KW   Iron-sulfur; Metal-binding; Nuclease; Nucleotide-binding.
FT   CHAIN           1..1169
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379199"
FT   DOMAIN          1..296
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   DOMAIN          276..582
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         804
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   1169 AA;  135538 MW;  04066AF30A7B39BB CRC64;
     MTLRIVSGRS GTGKSVFIHQ EIVEQLKSDP LGHPIFIIVP DQMSYSTEYE LTNRHGLQGL
     IRAQVMTFKR LAWLVLQETG GIARKEVNGY GYRMLIRKLL EEQKSEFSLF RQAAGKRGFT
     EEIETLLKEF SRYSVNSSVL AEVKESLKAI DAPNTLQAKT NDLYVVLQAL EERLGTTYVD
     SEGYYPILTE QLKYAETMKQ ATIYIDGFTA FTVRELELVR ELLKVTKHVT VVLPFDHIDE
     AFDEQALFHE AALTNQRLHD IANEEGIDVE PPLHFYYTQR FQSEDLQHVE ANFANMVPHT
     KKTSGDVMVF EASNRRAEVH AIAREITKLT REYGYRYQDI VLLYRQAELY DPLITSIFQQ
     YEIPIFTNTK KTMLHHPLIE LSRSALEIMT SNWKYEPVFR SVKTDLFFPL QAELTIWRER
     ADRLENYCLA QGIYGERWFE EPRWFYKKYR GLEFHSRVQT DEERAMQAEI EAIRDEIRQP
     LKSLQDKLSI ASTGKDIATA LFELVESLQV YEKLQAMKDR ELERGDALAA SEHEQAWNEW
     INVLDQFVYM FGEQEMSVEE AAKILDEGFD TLEFSRIPPT LDEVMVATVD LARLSNIKVA
     FVLGMNDGVY PTRMEYEGLL SDTEREWFSQ IGYELAPTSS NRLLQENFLF YRAASTPSNK
     LYLTYPTADE EGKALLSSLY IKKFIGNDKI AGLLSGVQAE RVVMDPIELL DESALPYLRH
     PRTALAHLMV QLRQAEHSRE LAPEWLALQK FYQQDPYWAL IFDRVHYPIT HKNEAEPLET
     YITQELYGQK LTSSVSRIEK YFRCPFSHFT TYGLRLEERA EYRLETFAMG DLFHEALKWI
     TEETHRLQLS WIRLTKQQIK QLARQAVEQI VPVFSHQILL SSARYRYIQR KLIRIVERTM
     MALTQHANVS HFKPIAIEAS FGPGQHEQLP PLEIDLTSGK KMFMRGRIDR IDSATIDDRS
     YLRIVDYKSS ARDLDLNEVY YGLSLQVLTY LDVAMENSTY WLPGETEPAG VLYVHVHNPM
     LKLDKDMTDS EIEEDRLKQY KMKGLLSENA ESILSMDEQL EESSGHSKII PVYMKKDGTP
     SESQSRIVPV NDMKRLQHFV RRKHQEAGNG ILSGDTAISP YKLKSKTACD YCQFAAVCQF
     DPSDGKQNYR QLMQAKPNEI VDKIRKEIE
 
 
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