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Database: UniProt
Entry: K6XYL6_9ALTE
LinkDB: K6XYL6_9ALTE
Original site: K6XYL6_9ALTE 
ID   K6XYL6_9ALTE            Unreviewed;       226 AA.
AC   K6XYL6;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Ribosomal protein S6 modification protein {ECO:0000313|EMBL:GAC16736.1};
GN   Name=rimK {ECO:0000313|EMBL:GAC16736.1};
GN   ORFNames=GLIP_4125 {ECO:0000313|EMBL:GAC16736.1};
OS   Aliiglaciecola lipolytica E3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Aliiglaciecola.
OX   NCBI_TaxID=1127673 {ECO:0000313|EMBL:GAC16736.1, ECO:0000313|Proteomes:UP000006334};
RN   [1] {ECO:0000313|EMBL:GAC16736.1, ECO:0000313|Proteomes:UP000006334}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E3 {ECO:0000313|EMBL:GAC16736.1,
RC   ECO:0000313|Proteomes:UP000006334};
RX   PubMed=25009843;
RA   Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA   Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT   "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT   high degree of genomic diversity and genomic characteristic for cold
RT   adaptation.";
RL   Environ. Microbiol. 16:1642-1653(2014).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAC16736.1}.
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DR   EMBL; BAEN01000076; GAC16736.1; -; Genomic_DNA.
DR   AlphaFoldDB; K6XYL6; -.
DR   STRING; 1127673.GLIP_4125; -.
DR   eggNOG; COG0189; Bacteria.
DR   Proteomes; UP000006334; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013651; ATP-grasp_RimK-type.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR004666; Rp_bS6_RimK/Lys_biosynth_LsyX.
DR   NCBIfam; TIGR00768; rimK_fam; 1.
DR   PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR   PANTHER; PTHR21621:SF7; RIBOSOMAL PROTEIN S6--L-GLUTAMATE LIGASE; 1.
DR   Pfam; PF08443; RimK; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006334}.
FT   DOMAIN          29..212
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   226 AA;  24153 MW;  D59BEB5F8F0E8C67 CRC64;
     MVRQFEMMGT FSINESVAIS RSRDKLRSLQ LLSRKGIGMP RTGFANHPDR IDDLIKNVGG
     APVVIKLLEG TQGIGVVLAE TQKAAESIIE AFMGLNASIL VQEFIKEAGG SDIRCLVVGG
     KVIAAMKRQA AEGEFRSNLH RGGTAKIVRL SPAERKTAVD AAKTMGLNMC GVDLLRSNHG
     PVVMEVNSSP GLEGIENATN KDIAGMIIEF IETNAKPHKT KTKGTG
//
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