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ADDA_LACJO
ID   ADDA_LACJO              Reviewed;        1204 AA.
AC   Q74JA6;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 120.
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=LJ_1203;
OS   Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=257314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNCM I-1225 / La1 / NCC 533;
RX   PubMed=14983040; DOI=10.1073/pnas.0307327101;
RA   Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C.,
RA   Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R.,
RA   Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.;
RT   "The genome sequence of the probiotic intestinal bacterium Lactobacillus
RT   johnsonii NCC 533.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004).
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; AE017198; AAS09024.1; -; Genomic_DNA.
DR   RefSeq; WP_011162032.1; NC_005362.1.
DR   AlphaFoldDB; Q74JA6; -.
DR   SMR; Q74JA6; -.
DR   STRING; 257314.LJ_1203; -.
DR   PRIDE; Q74JA6; -.
DR   EnsemblBacteria; AAS09024; AAS09024; LJ_1203.
DR   KEGG; ljo:LJ_1203; -.
DR   PATRIC; fig|257314.6.peg.1069; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   Proteomes; UP000000581; 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; Reference proteome.
FT   CHAIN           1..1204
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379284"
FT   DOMAIN          2..469
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          496..784
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   BINDING         23..30
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ   SEQUENCE   1204 AA;  139871 MW;  6049198AB96EA162 CRC64;
     MTKFTKEQNQ AINDYGKDIL VSASAGSGKT TVLVERVLKR ILSGTPVSSL LIITFTKAAA
     REMKERIKQK ISDQIEKEPN NQFLRSQLLD VDTANISTID SFCLDVIRRF YYVIDLDPQF
     SVLTDETQAE LLKERALHEI EIEYLEKNDQ DFQDFYDNFS GDRDAEGARN LLLQLYNTVV
     TEPNYEKFLN NLPNFYQVQD DLIESDLWQT QIKPLLIKEI KDLQTEIRQF FENPQMENPD
     LVKVKENYDI FTSRLEQFLN ALEDDHSYNE IRASLMNCKF EKNIRKSKKW SEESLETYQE
     SQKLKSDLND QLKKIFANFF VVEEKEQVNI LKKSEKLVKT IVDAEKKLIK RFGQLKREQN
     LIDYSDMEQF AFSILTTDTS NAHIAQEYYQ EKFNEILIDE YQDVNALQEN IIAAIKKKGQ
     NNLFMVGDIK QSIYGFRQAR PDLFLSKYHA YGQNDDSEKI VLSDNFRSTQ RVTKTVNSLF
     NPILTANFGG IDYKKEGQLQ FGATYYPTDL PTASEYIFTD KKQTQASFEE NFGDEMDFSE
     IQMVIARIKQ LKEENFQVWD RKTQLKRPLE YSDIAIITRT RSDNLQVMQE FAKADLPLFV
     TDAQNYFQTF ELVMIMNYLR LIDNPQQDIP LVAVLRSPLF NFKEPELAQI RVKTRSGNFY
     NALTSFASVN SDLGQKCKNF LQQLESLRSF AATHRISELI WSIYERTHLL EIVTGLPNGQ
     QRRVNLESLY ERATSYESAG FKGLYQFISF IERMRKNQKD LAQPLLSDKA DKAVKLMTIH
     ASKGLEFPVV FVMGLGHKYQ TRDLSGNFTI SKDGLGLTIK EKDYRIDSLV KSLADVEKRQ
     QMLEEEARIL YVGLTRAQQK LILVASVSEM EAKQKKWESE IDQKTNILPL IRKINAQSPL
     DFLGPKLEQK HEFDQTIEDM TLALEEQDKI YYLKFAVQSD IEEKDEQKDD TQKLSSKMND
     VVKTLYNFEY PFADATKTTA YQSVSEIKKV FNDPMDTELE NSRLISSSNR YLQPIDETPV
     FLEKQKFTGA EIGTAMHLVL QYYDYQGDKT EINLEQEIEE LVELGKLNPL MVPHLSKEAL
     NWFVMSEFAA EFWQKPEKLH RESQFSSLVN ASELFNDFSD SAAKILVHGT IDGYFETDEG
     LILFDYKTDF VDKTHEEQAI DKIKKKYTGQ LRLYEQALNE ISENKKVIGK YLILLDARKV
     VPVD
 
 
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