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Database: UniProt
Entry: B5UAT8
LinkDB: B5UAT8
Original site: B5UAT8 
ID   RIZA_BACIU              Reviewed;         413 AA.
AC   B5UAT8;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   05-DEC-2018, entry version 32.
DE   RecName: Full=L-arginine-specific L-amino acid ligase {ECO:0000305};
DE            EC=6.3.2.48 {ECO:0000269|PubMed:19352016};
DE   AltName: Full=L-amino acid ligase RizA {ECO:0000303|PubMed:19352016};
GN   Name=rizA {ECO:0000303|PubMed:19352016};
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-25, FUNCTION,
RP   CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBUNIT.
RC   STRAIN=ATCC 6633 / PCI 219 / NRS 231;
RX   PubMed=19352016; DOI=10.1271/bbb.80842;
RA   Kino K., Kotanaka Y., Arai T., Yagasaki M.;
RT   "A novel L-amino acid ligase from Bacillus subtilis NBRC3134, a
RT   microorganism producing peptide-antibiotic rhizocticin.";
RL   Biosci. Biotechnol. Biochem. 73:901-907(2009).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RC   STRAIN=ATCC 6633 / PCI 219 / NRS 231;
RX   PubMed=26323296; DOI=10.1107/S2053230X15012698;
RA   Kagawa W., Arai T., Ishikura S., Kino K., Kurumizaka H.;
RT   "Structure of RizA, an L-amino-acid ligase from Bacillus subtilis.";
RL   Acta Crystallogr. F 71:1125-1130(2015).
CC   -!- FUNCTION: Catalyzes the synthesis of Arg-Xaa dipeptides in an ATP-
CC       dependent manner. Has strict specificity toward arginine as the N-
CC       terminal substrate. {ECO:0000269|PubMed:19352016}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an L-alpha-amino acid + ATP + L-arginine = ADP + H(+) +
CC         L-arginyl-L-alpha-amino acid + phosphate; Xref=Rhea:RHEA:44336,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:59869, ChEBI:CHEBI:84315,
CC         ChEBI:CHEBI:456216; EC=6.3.2.48;
CC         Evidence={ECO:0000269|PubMed:19352016};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00409,
CC         ECO:0000269|PubMed:19352016};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00409,
CC         ECO:0000269|PubMed:19352016};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000269|PubMed:19352016};
CC       Note=Activity is maximal in the presence of Mg(2+). The use of
CC       Mn(2+) or Co(2+) decreases ligase activity.
CC       {ECO:0000269|PubMed:19352016};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 9.5. {ECO:0000269|PubMed:19352016};
CC       Temperature dependence:
CC         Optimum temperature is 37 degrees Celsius.
CC         {ECO:0000269|PubMed:19352016};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19352016}.
DR   EMBL; AB437349; BAG72134.1; -; Genomic_DNA.
DR   PDB; 4WD3; X-ray; 2.80 A; A/B=1-413.
DR   PDBsum; 4WD3; -.
DR   SMR; B5UAT8; -.
DR   KEGG; ag:BAG72134; -.
DR   KO; K22115; -.
DR   BioCyc; MetaCyc:MONOMER-18696; -.
DR   BRENDA; 6.3.2.28; 658.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cobalt; Direct protein sequencing; Ligase;
KW   Magnesium; Manganese; Metal-binding; Nucleotide-binding.
FT   CHAIN         1    413       L-arginine-specific L-amino acid ligase.
FT                                /FTId=PRO_0000434829.
FT   DOMAIN      115    312       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   NP_BIND     141    202       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   METAL       268    268       Magnesium or manganese.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       281    281       Magnesium or manganese.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   STRAND        2      7       {ECO:0000244|PDB:4WD3}.
FT   HELIX        12     24       {ECO:0000244|PDB:4WD3}.
FT   STRAND       28     34       {ECO:0000244|PDB:4WD3}.
FT   HELIX        36     41       {ECO:0000244|PDB:4WD3}.
FT   TURN         42     45       {ECO:0000244|PDB:4WD3}.
FT   STRAND       47     51       {ECO:0000244|PDB:4WD3}.
FT   HELIX        58     71       {ECO:0000244|PDB:4WD3}.
FT   STRAND       75     79       {ECO:0000244|PDB:4WD3}.
FT   HELIX        82     84       {ECO:0000244|PDB:4WD3}.
FT   HELIX        85     94       {ECO:0000244|PDB:4WD3}.
FT   STRAND       98    100       {ECO:0000244|PDB:4WD3}.
FT   HELIX       102    107       {ECO:0000244|PDB:4WD3}.
FT   HELIX       111    121       {ECO:0000244|PDB:4WD3}.
FT   STRAND      129    132       {ECO:0000244|PDB:4WD3}.
FT   HELIX       134    136       {ECO:0000244|PDB:4WD3}.
FT   HELIX       137    144       {ECO:0000244|PDB:4WD3}.
FT   STRAND      146    155       {ECO:0000244|PDB:4WD3}.
FT   TURN        158    160       {ECO:0000244|PDB:4WD3}.
FT   STRAND      162    164       {ECO:0000244|PDB:4WD3}.
FT   HELIX       167    175       {ECO:0000244|PDB:4WD3}.
FT   TURN        177    180       {ECO:0000244|PDB:4WD3}.
FT   HELIX       181    185       {ECO:0000244|PDB:4WD3}.
FT   STRAND      190    194       {ECO:0000244|PDB:4WD3}.
FT   STRAND      199    208       {ECO:0000244|PDB:4WD3}.
FT   STRAND      211    220       {ECO:0000244|PDB:4WD3}.
FT   STRAND      232    236       {ECO:0000244|PDB:4WD3}.
FT   HELIX       244    257       {ECO:0000244|PDB:4WD3}.
FT   STRAND      262    271       {ECO:0000244|PDB:4WD3}.
FT   STRAND      277    285       {ECO:0000244|PDB:4WD3}.
FT   HELIX       290    299       {ECO:0000244|PDB:4WD3}.
FT   HELIX       303    311       {ECO:0000244|PDB:4WD3}.
FT   STRAND      324    332       {ECO:0000244|PDB:4WD3}.
FT   STRAND      336    338       {ECO:0000244|PDB:4WD3}.
FT   HELIX       345    349       {ECO:0000244|PDB:4WD3}.
FT   STRAND      354    361       {ECO:0000244|PDB:4WD3}.
FT   STRAND      378    387       {ECO:0000244|PDB:4WD3}.
FT   HELIX       388    400       {ECO:0000244|PDB:4WD3}.
SQ   SEQUENCE   413 AA;  46345 MW;  12A2229ADE4E066B CRC64;
     MLRILLINSD KPEPIQFFQK DKETNDSINI SVITRSCYAP LYSHWADHVY IVDDVTDLTV
     MKSLMLEILK VGPFDHIVST TEKSILTGGF LRSYFGIAGP GFETALYMTN KLAMKTKLKM
     EGIPVADFLC VSQVEDIPAA GEKLGWPIIV KPALGSGALN TFIIHSLDHY EDLYSTSGGL
     GELKKNNSLM IAEKCIEMEE FHCDTLYADG EILFVSISKY TVPLLKGMAK IQGSFILSQN
     DPVYAEILEL QKSVAQAFRI TDGPGHLEIY RTHSGELIVG EIAMRIGGGG ISRMIEKKFN
     ISLWESSLNI SVYRDPNLTV NPIEGTVGYF SLPCRNGTIK EFTPIEEWEK LAGILEVELL
     YQEGDVVDEK QSSSFDLARL YFCLENENEV QHLLALVKQT YYLHLTEDHM MNQ
//
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