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Database: UniProt
Entry: A0A1I1Q8A3_9BACT
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Original site: A0A1I1Q8A3_9BACT 
ID   A0A1I1Q8A3_9BACT        Unreviewed;       302 AA.
AC   A0A1I1Q8A3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=SSU ribosomal protein S6P modification protein {ECO:0000313|EMBL:SFD16068.1};
GN   ORFNames=SAMN05216167_103568 {ECO:0000313|EMBL:SFD16068.1};
OS   Spirosoma endophyticum.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX   NCBI_TaxID=662367 {ECO:0000313|EMBL:SFD16068.1, ECO:0000313|Proteomes:UP000198598};
RN   [1] {ECO:0000313|EMBL:SFD16068.1, ECO:0000313|Proteomes:UP000198598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26130 {ECO:0000313|EMBL:SFD16068.1,
RC   ECO:0000313|Proteomes:UP000198598};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOLQ01000003; SFD16068.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1Q8A3; -.
DR   STRING; 662367.SAMN05216167_103568; -.
DR   OrthoDB; 3865600at2; -.
DR   Proteomes; UP000198598; 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:InterPro.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
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; IPR041107; Rimk_N.
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   Pfam; PF18030; Rimk_N; 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   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198598}.
FT   DOMAIN          104..289
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   302 AA;  32308 MW;  221BCEF72D202E42 CRC64;
     MRIAILSANP NLYSTQRLLE AASQRGHEGI IVNHLNCQVM IEGGRPSVLY EGQELDALDA
     IVPRIGASVT DYGCAVVRQF EMMNIFTTGK SQAIMRSRNK LRSLQVLSKA GVGLPKTMFA
     NHPKNGDITQ LIKRVGGPPV VIKLLEGTQG IGVVLAETTK AAKSTIEAFY GLKKNVLVQE
     FIAEAKGSDI RAFVIGGRVV GAIKRQGLDG DFRSNIHRGG NAVSIELTPQ EEQTAIQAAR
     ALGLKVAGVD MLPSERGPLV LEVNSSPGLE GIENATGVDI AIQIITYIED KIRTDEGDTV
     GV
//
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