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Database: UniProt
Entry: A9L4I9
LinkDB: A9L4I9
Original site: A9L4I9 
ID   RIMK2_SHEB9             Reviewed;         301 AA.
AC   A9L4I9;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   16-JAN-2019, entry version 72.
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=Sbal195_3945;
OS   Shewanella baltica (strain OS195).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=399599;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS195;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Brettar I., Rodrigues J., Konstantinidis K., Klappenbach J.,
RA   Hofle M., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS195.";
RL   Submitted (NOV-2007) 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; CP000891; ABX51105.1; -; Genomic_DNA.
DR   RefSeq; WP_006084244.1; NC_009997.1.
DR   EnsemblBacteria; ABX51105; ABX51105; Sbal195_3945.
DR   GeneID; 11773948; -.
DR   KEGG; sbn:Sbal195_3945; -.
DR   HOGENOM; HOG000293092; -.
DR   KO; K05844; -.
DR   OMA; NYLRCYM; -.
DR   BioCyc; SBAL399599:G1GAL-4135-MONOMER; -.
DR   Proteomes; UP000000770; Chromosome.
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; Complete proteome; Ligase; Magnesium; Manganese;
KW   Metal-binding; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    301       Probable alpha-L-glutamate ligase 2.
FT                                /FTId=PRO_0000340553.
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;  32439 MW;  52F65E528D0C6C34 CRC64;
     MKIGILSQFP QLYSTQRLVE ACQSRGHEAV VINTLNCYMN INSIKPSIHY EGTELVGFDA
     IIPRIHASVT FYGCAVVRQF EMMGVYAAND SISIARSRDK LRALQLLSRK GIGMPVTGFA
     NKPNDIPDLI NMVGGAPLVI KLLEGTQGIG VVLAETKTAA ESVIEAFLGL KANILVQEYI
     KESNGSDIRC FVVGDKVIAS MKRQGPEGDF RSNLHLGGCG EVVKITAVER KMAIAAVKAM
     GLVVAGVDIL RSNRGPLILE VNSAPGIEGI EQTTGISVTE PIVEYIEKMV SARKTNRPII
     A
//
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