ID RIMK_XANC5 Reviewed; 295 AA.
AC Q3BQ65;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 01-MAY-2013, entry version 53.
DE RecName: Full=Ribosomal protein S6 modification protein;
GN Name=rimK; OrderedLocusNames=XCV3367;
OS Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=316273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=85-10;
RX PubMed=16237009; DOI=10.1128/JB.187.21.7254-7266.2005;
RA Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O.,
RA Schneiker S., Schuster S.C., Vorhoelter F.J., Weber E., Puehler A.,
RA Bonas U., Bartels D., Kaiser O.;
RT "Insights into genome plasticity and pathogenicity of the plant
RT pathogenic Bacterium Xanthomonas campestris pv. vesicatoria revealed
RT by the complete genome sequence.";
RL J. Bacteriol. 187:7254-7266(2005).
CC -!- FUNCTION: Responsible for the addition of glutamate residues to
CC the C-terminus of ribosomal protein S6 (By similarity).
CC -!- COFACTOR: Binds 2 magnesium or manganese ions per subunit (By
CC similarity).
CC -!- SIMILARITY: Belongs to the RimK family.
CC -!- SIMILARITY: Contains 1 ATP-grasp domain.
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DR EMBL; AM039952; CAJ25098.1; -; Genomic_DNA.
DR RefSeq; YP_365098.1; NC_007508.1.
DR ProteinModelPortal; Q3BQ65; -.
DR STRING; 316273.XCV3367; -.
DR EnsemblBacteria; CAJ25098; CAJ25098; XCV3367.
DR GeneID; 3730221; -.
DR KEGG; xcv:XCV3367; -.
DR PATRIC; 24096340; VBIXanCam71633_3640.
DR eggNOG; COG0189; -.
DR HOGENOM; HOG000293092; -.
DR KO; K05844; -.
DR OMA; CREPRLY; -.
DR ProtClustDB; CLSK451700; -.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR GO; GO:0006464; P:cellular protein modification process; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:HAMAP.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.30.470.20; -; 1.
DR Gene3D; 3.40.50.20; -; 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; IPR013816; ATP_grasp_subdomain_2.
DR InterPro; IPR016185; PreATP-grasp_dom.
DR InterPro; IPR023533; Ribosomal_S6_modifier_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; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1 295 Ribosomal protein S6 modification
FT protein.
FT /FTId=PRO_0000205495.
FT DOMAIN 104 287 ATP-grasp.
FT NP_BIND 177 187 ATP (By similarity).
FT METAL 248 248 Magnesium or manganese 1 (By similarity).
FT METAL 260 260 Magnesium or manganese 1 (By similarity).
FT METAL 260 260 Magnesium or manganese 2 (By similarity).
FT METAL 262 262 Magnesium or manganese 2 (By similarity).
FT BINDING 141 141 ATP (By similarity).
FT BINDING 203 203 ATP (By similarity).
SQ SEQUENCE 295 AA; 31637 MW; 3AF58805CB9A3372 CRC64;
MKIAILSRNS KLYSTRRLIE AGRKRGHTVR ILDPLRCYMR IAADGFSLHY KGKPITGFDA
VIPRIGASVT RYATAVLRQL EFMGTYTPNP SDAILRSRDK LRAHQLLAAQ GIDMPVTVFG
DNPDDTQDLL SMLGPPPHVV KLNEGAQGAG VILTEKASAS RGVVEALRGL YANFIVQEFI
GEAEGADLRC FVVGDKVVAA MRRQAAEGDF RSNLHLGGTA AVTEATEQEQ EVAVRSARAL
GLTVAGVDLI RSKRGPLVLE VNSTPGLEGV EGVCGVDVAA AIVQHLEQSV RRSAG
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