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ADDB_STAA1
ID   ADDB_STAA1              Reviewed;        1157 AA.
AC   A7X0I1;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, 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}; OrderedLocusNames=SAHV_0961;
OS   Staphylococcus aureus (strain Mu3 / ATCC 700698).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=418127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu3 / ATCC 700698;
RX   PubMed=17954695; DOI=10.1128/aac.00534-07;
RA   Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.;
RT   "Mutated response regulator graR is responsible for phenotypic conversion
RT   of Staphylococcus aureus from heterogeneous vancomycin-intermediate
RT   resistance to vancomycin-intermediate resistance.";
RL   Antimicrob. Agents Chemother. 52:45-53(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; AP009324; BAF77844.1; -; Genomic_DNA.
DR   RefSeq; WP_000172350.1; NC_009782.1.
DR   AlphaFoldDB; A7X0I1; -.
DR   SMR; A7X0I1; -.
DR   KEGG; saw:SAHV_0961; -.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OMA; DRLENYV; -.
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; 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..1157
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379210"
FT   DOMAIN          1..275
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   DOMAIN          269..583
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         784
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1112
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1115
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1121
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ   SEQUENCE   1157 AA;  134357 MW;  EC09A392895A82C7 CRC64;
     MTLHAYLGRA GTGKSTKMLT EIKQKMKADP LGDPIILIAP TQSTFQLEQA FVNDPELNGS
     LRTEVLHFER LSHRIFQEVG SYSEQKLSKA ATEMMIYNIV QEQQKYLKLY QSQAKYYGFS
     EKLTEQIQDF KKYAVTPEHL EHFIADKNMQ TRTKNKLEDI ALIYREFEQR IQNEFITGED
     SLQYFIDCMP KSEWLKRADI YIDGFHNFST IEYLIIKGLI KYAKSVTIIL TTDGNHDQFS
     LFRKPSEVLR HIEEIANELN ISIERQYFNQ LYRFNNQDLK HLEQEFDVLQ INRVACQGHI
     NILESATMRE EINEIARRII VDIRDKQLRY QDIAILYRDE SYAYLFDSIL PLYNIPYNID
     TKRSMTHHPV MEMIRSLIEV IQSNWQVNPM LRLLKTDVLT ASYLKSAYLV DLLENFVLER
     GIYGKRWLDD ELFNVEHFSK MGRKAHKLTE DERNTFEQVV KLKKDVIDKI LHFEKQMSQA
     ETVKDFATAF YESMEYFELP NQLMTERDEL DLNGNHEKAE EIDQIWNGLI QILDDLVLVF
     GDEPMSMERF LEVFDIGLEQ LEFVMIPQTL DQVSIGTMDL AKVDNKQHVY LVGMNDGTMP
     QPVTASSLIT DEEKKYFEQQ ANVELSPTSD ILQMDEAFVC YVAMTRAKGD VTFSYSLMGS
     SGDDKEISPF LNQIQSLFNQ LEITNIPQYH EVNPLSLMQH AKQTKITLFE ALRAWLDDEI
     VADSWLDAYQ VIRDSDHLNQ GLDYLMSALT FDNETVKLGE TLSKDLYGKE INASVSRFEG
     YQQCPFKHYA SHGLKLNERT KYELQNFDLG DIFHSVLKYI SERINGDFKQ LDLKKIRQLT
     NEALEEILPK VQFNLLNSSA YYRYLSRRIG AIVETTLSAL KYQGTYSKFM PKHFETSFRR
     KPRTNDELIA QTLTTTQGIP INIRGQIDRI DTYTKNDTSF VNIIDYKSSE GSATLDLTKV
     YYGMQMQMMT YMDIVLQNKQ RLGLTDIVKP GGLLYFHVHE PRIKFKSWSD IDEDKLEQDL
     IKKFKLSGLV NADQTVIDAL DIRLEPKFTS DIVPVGLNKD GSLSKRGSQV ADEATIYKFI
     QHNKENFIET ASNIMDGHTE VAPLKYKQKL PCAFCSYQSV CHVDGMIDSK RYRTVDETIN
     PIEAIQNINI NDEFGGE
 
 
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