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Database: UniProt
Entry: Q5X7X4
LinkDB: Q5X7X4
Original site: Q5X7X4 
ID   RIMK_LEGPA              Reviewed;         302 AA.
AC   Q5X7X4;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   16-JAN-2019, entry version 88.
DE   RecName: Full=Probable alpha-L-glutamate ligase {ECO:0000255|HAMAP-Rule:MF_01552};
DE            EC=6.3.2.- {ECO:0000255|HAMAP-Rule:MF_01552};
GN   Name=rimK {ECO:0000255|HAMAP-Rule:MF_01552};
GN   OrderedLocusNames=lpp0481;
OS   Legionella pneumophila (strain Paris).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Paris;
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F.,
RA   Etienne J., Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of
RT   host cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(2004).
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; CR628336; CAH11629.1; -; Genomic_DNA.
DR   RefSeq; WP_010946163.1; NC_006368.1.
DR   ProteinModelPortal; Q5X7X4; -.
DR   SMR; Q5X7X4; -.
DR   PRIDE; Q5X7X4; -.
DR   EnsemblBacteria; CAH11629; CAH11629; lpp0481.
DR   KEGG; lpp:lpp0481; -.
DR   LegioList; lpp0481; -.
DR   eggNOG; ENOG4105D9I; Bacteria.
DR   eggNOG; COG0189; LUCA.
DR   HOGENOM; HOG000293092; -.
DR   KO; K05844; -.
DR   OMA; NYLRCYM; -.
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    302       Probable alpha-L-glutamate ligase.
FT                                /FTId=PRO_0000205463.
FT   DOMAIN      105    288       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_01552}.
FT   NP_BIND     179    180       ATP. {ECO:0000255|HAMAP-Rule:MF_01552}.
FT   NP_BIND     212    214       ATP. {ECO:0000255|HAMAP-Rule:MF_01552}.
FT   METAL       249    249       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01552}.
FT   METAL       261    261       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01552}.
FT   METAL       261    261       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01552}.
FT   METAL       263    263       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01552}.
FT   BINDING     142    142       ATP. {ECO:0000255|HAMAP-Rule:MF_01552}.
FT   BINDING     188    188       ATP. {ECO:0000255|HAMAP-Rule:MF_01552}.
SQ   SEQUENCE   302 AA;  32881 MW;  DA9A2689AADD2B10 CRC64;
     MKIAILATNP HLYSHKRLKA EAEAAGHEVK IINPLYCYMN VAASNPKVHY RGGAPLPHFD
     AVIPRIGASI TYYGTAVLRH METMGMYTLN ESIAISRSRD KFRSLQLLAR KGIPMPLTSF
     AQSPDDTEDL IHMVGGAPLV IKLLEGTQGK GVILADSHQS AVSIINAFKE MHANILVQEF
     IEESRGTDIR CFVIGEKVVA AVKRQAKDGE FRANVHQGGK AVKVKLSPQE RAIAVSAAKT
     MGLRVAGVDL IRSNHGPLVL EINSSPGLEG IEKATNINLA GKIIEYIEKK AKPISSNHRF
     HG
//
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