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ADDA_BACVZ
ID   ADDA_BACVZ              Reviewed;        1235 AA.
AC   A7Z368;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=ATP-dependent helicase/nuclease subunit A {ECO:0000255|HAMAP-Rule:MF_01451};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01451};
DE            EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01451};
DE   AltName: Full=ATP-dependent helicase/nuclease AddA {ECO:0000255|HAMAP-Rule:MF_01451};
GN   Name=addA {ECO:0000255|HAMAP-Rule:MF_01451}; OrderedLocusNames=RBAM_010800;
OS   Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS   (Bacillus amyloliquefaciens subsp. plantarum).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=326423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX   PubMed=17704766; DOI=10.1038/nbt1325;
RA   Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA   Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA   Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA   Strittmatter A., Gottschalk G., Borriss R.;
RT   "Comparative analysis of the complete genome sequence of the plant growth-
RT   promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Nat. Biotechnol. 25:1007-1014(2007).
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 AddA nuclease domain is
CC       required for chi fragment generation; this subunit has the helicase and
CC       3' -> 5' nuclease activities. {ECO:0000255|HAMAP-Rule:MF_01451}.
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_01451};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01451};
CC   -!- SUBUNIT: Heterodimer of AddA and AddB/RexB. {ECO:0000255|HAMAP-
CC       Rule:MF_01451}.
CC   -!- SIMILARITY: Belongs to the helicase family. AddA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01451}.
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DR   EMBL; CP000560; ABS73444.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7Z368; -.
DR   SMR; A7Z368; -.
DR   STRING; 326423.RBAM_010800; -.
DR   EnsemblBacteria; ABS73444; ABS73444; RBAM_010800.
DR   KEGG; bay:RBAM_010800; -.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   Proteomes; UP000001120; Chromosome.
DR   GO; GO:0008408; F:3'-5' 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-UniRule.
DR   GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
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_01451; AddA; 1.
DR   InterPro; IPR014152; DNA_helicase_suAddA.
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   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070; PTHR11070; 1.
DR   PANTHER; PTHR11070:SF48; PTHR11070:SF48; 1.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF52980; SSF52980; 1.
DR   TIGRFAMs; TIGR02785; addA_Gpos; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA repair; DNA-binding; Exonuclease; Helicase;
KW   Hydrolase; Nuclease; Nucleotide-binding.
FT   CHAIN           1..1235
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379230"
FT   DOMAIN          10..482
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          509..799
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   BINDING         31..38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ   SEQUENCE   1235 AA;  141321 MW;  0DF44334A1F2FA2F CRC64;
     MMQIPKPKDS IWTDDQWSAI VSSGRDILVA AAAGSGKTAV LVERMIRKIT AEEDPVDVDR
     LLVVTFTNAS AAEMKHRIAE ALEKELAKNP GSLHIRRQLS LLNRASISTL HSFCLQVLKK
     YYYMIDLDPG FRMADQTEGE LLGDEVLDEL FEDEYAKGNQ AFFELADRYT TDRHDLDLQD
     LVKRVYEYSR SHPDPEVWLQ SFVRLYDVTE ESKMEELPFY QYVKEDAEMA LFGAKQKLEK
     ALELTKAPGG PAPRADNFLD DLQQIEELIS CRHDFDALYE RVPAVSFKRA KAVKGDEFDK
     ALLDEATDLR NGAKKLIEKV KTDYFTRSPQ DHLKSLADMK PVIETLVQLV ISYGKRFEAA
     KQEKSIIDFS DLEHYCLAIL TAVDEEGRRV PSEAAVYYQD QFHEVLVDEY QDTNLVQESI
     LQLVKSGNEE AGNLFMVGDV KQSIYRFRLA EPLLFLGKYK RFTESGAGAG QKIDLNQNFR
     SRSDILDSTN FLFKQLMGGK IGEVDYDEQA ALKLGASYPP NDAAKTELLL IDSADGADSS
     EDAEDFETVH WEAKAIAGEI RKLVSSPFKV YDGKTKTHRN IQYRDIVILL RSMPWAPQLM
     EELKNQGIPV YANLTSGYFE AVEVAAALSV LKVIDNPYQD IPLASVLRSP IVGCDENELA
     LIRLEKKKAP FYEALKAYLA NADRHDELYQ KLRTFYDSLQ KWRSFSTNHS VSELIWEVYR
     DTGYFDYAGG MPGGKQRQAN LRVLYDRARS YEATAFRGLF RFLRFIERMQ ERGDDLGTAR
     ALSEQEDVVR LMTIHSSKGL EFPVVFTAGL GRSFNMMDLN KSYLLDKELG FGTKYIHPEL
     RISYPTLPLV AMKKKMRREL LSEELRVLYV ALTRAKEKLF LVGSCKNREK QLAKWQAQAD
     RADWLLSEFD RYQASSYLDF IGPALIRHRD MEAHRTPGLS SSEDIARDPS RFHIRMLQQS
     ELLEENPKER AEEKSKRLKA IQQGEPIPDS FSFDDQARRL LEWEYPYREL TAIRTKQSVS
     ELKRKQEYED EYSGRSLIKP SGDTLLYRRP GFMMKKGLTA AEKGTAMHTV MQHIPLTHVP
     TAEEAERTVR MLYEKELLTE EQQEAIDIEE IVQFFGTEIG KDLLRALRID REVPFSMALP
     AGEVYKDAET AGEPLLVQGI IDCLYETADG LYLLDYKTDR IEGKFRNGFE GAAPILQKRY
     ETQIELYTKA VEQITKTKVK GRALYFFDGG HVLTL
 
 
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