RIMK_PARMW
ID RIMK_PARMW Reviewed; 466 AA.
AC Q7U6F4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Probable alpha-L-glutamate ligase;
DE EC=6.3.2.-;
GN Name=rimK; OrderedLocusNames=SYNW1384;
OS Parasynechococcus marenigrum (strain WH8102).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Parasynechococcus; Parasynechococcus marenigrum.
OX NCBI_TaxID=84588;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH8102;
RX PubMed=12917641; DOI=10.1038/nature01943;
RA Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT "The genome of a motile marine Synechococcus.";
RL Nature 424:1037-1042(2003).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
CC -!- SIMILARITY: In the C-terminal section; belongs to the RimK family.
CC {ECO:0000305}.
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DR EMBL; BX569692; CAE07899.1; -; Genomic_DNA.
DR RefSeq; WP_011128248.1; NC_005070.1.
DR AlphaFoldDB; Q7U6F4; -.
DR SMR; Q7U6F4; -.
DR STRING; 84588.SYNW1384; -.
DR EnsemblBacteria; CAE07899; CAE07899; SYNW1384.
DR KEGG; syw:SYNW1384; -.
DR eggNOG; COG0189; Bacteria.
DR eggNOG; COG4067; Bacteria.
DR HOGENOM; CLU_045509_1_1_3; -.
DR OMA; PELYSNK; -.
DR OrthoDB; 359914at2; -.
DR Proteomes; UP000001422; Chromosome.
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 GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; -; 1.
DR Gene3D; 3.30.1490.20; -; 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; 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..466
FT /note="Probable alpha-L-glutamate ligase"
FT /id="PRO_0000205486"
FT DOMAIN 266..449
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT REGION 1..161
FT /note="Unknown"
FT REGION 162..466
FT /note="Alpha-L-glutamate ligase"
FT BINDING 303
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 340..341
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 349
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 373..375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 410
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 410
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 422
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 422
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 422
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 422
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 424
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 424
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
SQ SEQUENCE 466 AA; 51437 MW; BF810994693F0CE8 CRC64;
MTRKIIVGSE EWCSLPGLGL PAIKARVDSG AATSSLHAFN IVPFQRDEAR WISFEVHPLQ
NDRSVVIRRE SPVLEQRGVR NTSGITETRY VIREQLVLGE ESWPIELTLT NRDAMGYRML
LGREAMVGRV LVDPEGSHQL GDLRQDQLEA MYAPLRTERN GLRIALLASD PELYSNRRLL
EAGEERGHRM EFLNVKQCYM RLDPQNPEMH YRGGNVLERI NAVIPRIRPS VTFYGCAITR
QFEAMGISVL NAAEPIKRSR DKLLASQLFV RHGLNMPVTG FASSPLDTKD LIKMVGGAPL
ILKLLEGAQG RGVVLAETQK AAESVINAMK SLNANLLVQE FIKEAGGKDL RCFVIGGKVV
SAIERTAAVG DFRSNIHQGG SAQAVRIRPE ERKLAVSATR ALGLDVAGVD IIRSERGPLL
LEVNSSPGLE GIETATGKDL AGLMIQEIER KLGWVRTRLS EPQVAC
