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RIMK_SHEHH
ID   RIMK_SHEHH              Reviewed;         458 AA.
AC   B0TTR5;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
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}; OrderedLocusNames=Shal_2072;
OS   Shewanella halifaxensis (strain HAW-EB4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=458817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL   Submitted (JAN-2008) 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: In the C-terminal section; belongs to the RimK family.
CC       {ECO:0000305}.
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DR   EMBL; CP000931; ABZ76633.1; -; Genomic_DNA.
DR   RefSeq; WP_012277163.1; NC_010334.1.
DR   AlphaFoldDB; B0TTR5; -.
DR   SMR; B0TTR5; -.
DR   STRING; 458817.Shal_2072; -.
DR   PRIDE; B0TTR5; -.
DR   EnsemblBacteria; ABZ76633; ABZ76633; Shal_2072.
DR   KEGG; shl:Shal_2072; -.
DR   eggNOG; COG0189; Bacteria.
DR   eggNOG; COG4067; Bacteria.
DR   HOGENOM; CLU_045509_1_1_6; -.
DR   OMA; CYMNIAS; -.
DR   Proteomes; UP000001317; 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:0006412; P:translation; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.70.10; -; 1.
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; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR008503; Put_Zn_protease.
DR   InterPro; IPR023533; RimK.
DR   InterPro; IPR041107; Rimk_N.
DR   InterPro; IPR004666; RpS6_RimK/Lys_biosynth_LsyX.
DR   Pfam; PF08443; RimK; 1.
DR   Pfam; PF18030; Rimk_N; 1.
DR   Pfam; PF05618; Zn_protease; 1.
DR   SUPFAM; SSF50630; SSF50630; 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..458
FT                   /note="Probable alpha-L-glutamate ligase"
FT                   /id="PRO_0000340570"
FT   DOMAIN          267..450
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01552"
FT   REGION          1..162
FT                   /note="Unknown"
FT   REGION          163..458
FT                   /note="Alpha-L-glutamate ligase"
FT   BINDING         304
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01552"
FT   BINDING         341..342
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01552"
FT   BINDING         350
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01552"
FT   BINDING         374..376
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01552"
FT   BINDING         411
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01552"
FT   BINDING         411
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01552"
FT   BINDING         423
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01552"
FT   BINDING         423
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01552"
FT   BINDING         423
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01552"
FT   BINDING         423
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01552"
FT   BINDING         425
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01552"
FT   BINDING         425
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01552"
SQ   SEQUENCE   458 AA;  50125 MW;  FD2535E1CF89601A CRC64;
     MSDNKFIIGS EEWCAFPALG VPAIKARVDS GARTSSIHAV NIRPFKREGE PWVSFELHPI
     QNSRKIILRC ESKVIDRRNI KSSNGEIEKR YVIASVIQLG GHAWEVELTL TNRDSMGYRM
     LLGREAMSNK TLVDPSESFC LGQQNDVEVE QLYGVKSAKK SGLKIGLLAS NPDLYSNRRI
     IEAGEQRGHE MVFLNIKQCY LKLDASEPEV HYRGGRILND LDAVIPRIRP SMTFYGCALT
     RHFESLNIMA LNTSDAITRS RDKLFSLQLL QKNNLDIPTS GFANSPVDTK DLIDMVGGAP
     LIVKLLEGTQ GKGVVLAETT KAAESVINAF KSLHVNLLVQ EFIKEAQGKD LRCFVIDGKV
     VASIERTAAP GEFRANIHQG GSASIVSVSA AERQLALKAA KTMGLRVAGV DIIRSSRGPL
     LLEINSSPGL EGIESATGID IAGAMIDSIE KKLGWKAE
 
 
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