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Database: UniProt
Entry: A1RJ58
LinkDB: A1RJ58
Original site: A1RJ58 
ID   RIMK2_SHESW             Reviewed;         301 AA.
AC   A1RJ58;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   13-FEB-2019, entry version 70.
DE   RecName: Full=Probable alpha-L-glutamate ligase 2 {ECO:0000255|HAMAP-Rule:MF_01552};
DE            EC=6.3.2.- {ECO:0000255|HAMAP-Rule:MF_01552};
GN   Name=rimK2 {ECO:0000255|HAMAP-Rule:MF_01552};
GN   OrderedLocusNames=Sputw3181_1868;
OS   Shewanella sp. (strain W3-18-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=351745;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W3-18-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of Shewanella sp. W3-18-1.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01552};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01552};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_01552};
CC   -!- SIMILARITY: Belongs to the RimK family. {ECO:0000255|HAMAP-
CC       Rule:MF_01552}.
DR   EMBL; CP000503; ABM24703.1; -; Genomic_DNA.
DR   RefSeq; WP_011789195.1; NC_008750.1.
DR   SMR; A1RJ58; -.
DR   EnsemblBacteria; ABM24703; ABM24703; Sputw3181_1868.
DR   KEGG; shw:Sputw3181_1868; -.
DR   HOGENOM; HOG000293092; -.
DR   KO; K05844; -.
DR   OMA; YEHKVFY; -.
DR   BioCyc; SSP351745:G1G7O-1960-MONOMER; -.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006464; P:cellular protein modification process; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   HAMAP; MF_01552; RimK; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013651; ATP-grasp_RimK-type.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR023533; RimK.
DR   InterPro; IPR004666; RpS6_RimK/Lys_biosynth_LsyX.
DR   Pfam; PF08443; RimK; 1.
DR   TIGRFAMs; TIGR00768; rimK_fam; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    301       Probable alpha-L-glutamate ligase 2.
FT                                /FTId=PRO_0000340567.
FT   DOMAIN      104    287       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_01552}.
FT   NP_BIND     178    179       ATP. {ECO:0000255|HAMAP-Rule:MF_01552}.
FT   NP_BIND     211    213       ATP. {ECO:0000255|HAMAP-Rule:MF_01552}.
FT   METAL       248    248       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01552}.
FT   METAL       260    260       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01552}.
FT   METAL       260    260       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01552}.
FT   METAL       262    262       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01552}.
FT   BINDING     141    141       ATP. {ECO:0000255|HAMAP-Rule:MF_01552}.
FT   BINDING     187    187       ATP. {ECO:0000255|HAMAP-Rule:MF_01552}.
SQ   SEQUENCE   301 AA;  32483 MW;  13E364035073AB54 CRC64;
     MRIAILSQGP ELYSTKRLVE AAQLRGHEVH VINPLECYMN INMRQSSIHI GGRELPTFDA
     VIPRIGASIT FYGSAVLRQF EMMGVYALND SVGISRSRDK LRSMQLMSRR GIGLPITGFA
     NKPSDIPDLI DMVGGAPLVI KLLEGTQGIG VVLAETRKAA ESVIEAFMGL KANIMVQEYI
     KEANGADIRC FVLGDKVIAA MKRQAMPGEF RSNLHRGGTA SLVKLTPEER SVAIRAAKTM
     GLNVAGVDLL RSNHGPVIME VNSSPGLEGI EGATTKDVAG AIIEFVEKNV TKVKKVTQAQ
     G
//
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