ID   A0A1G8SFE6_9RHOB        Unreviewed;       477 AA.
AC   A0A1G8SFE6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=SSU ribosomal protein S6P modification protein {ECO:0000313|EMBL:SDJ27897.1};
GN   ORFNames=SAMN04487993_102437 {ECO:0000313|EMBL:SDJ27897.1};
OS   Salipiger marinus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Salipiger.
OX   NCBI_TaxID=555512 {ECO:0000313|EMBL:SDJ27897.1, ECO:0000313|Proteomes:UP000199093};
RN   [1] {ECO:0000313|EMBL:SDJ27897.1, ECO:0000313|Proteomes:UP000199093}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26424 {ECO:0000313|EMBL:SDJ27897.1,
RC   ECO:0000313|Proteomes:UP000199093};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNEJ01000024; SDJ27897.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8SFE6; -.
DR   STRING; 555512.SAMN04487993_102437; -.
DR   OrthoDB; 3865600at2; -.
DR   Proteomes; UP000199093; 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; 2.40.70.10; Acid Proteases; 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; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR008503; Put_Zn_protease.
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   Pfam; PF05618; Zn_protease; 1.
DR   SUPFAM; SSF50630; Acid proteases; 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:UP000199093}.
FT   DOMAIN          263..446
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   REGION          448..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        450..466
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   477 AA;  52064 MW;  CC8D11E8B2EE46BF CRC64;
     MPQFTLGWEE WLSLPDLDLP AIRAKVDTGA KTSALHAFAI EPFGSAERPM VRFAIHPDPQ
     DTGLEIICSA PLKDRREITS SNGETEMRFV IETDVTMGGR TWPIEVTLTD RGGMAYRMLL
     GRSALLPEMI VAPAQRLQQP QLSYDVYHAS LRQRPHRRAL RLAILTREAE NYSTRRLIEA
     AEARGHTMEV IDTSRCYMNI RAIGGEVHYD GRPLPHYDAV IPRIGASITS YGTAVVRQFE
     SLGTYCLAGS EGITVSRDKL HAHQVLARHR IGMPTTAFAR SPKDSGNVIA VVGGAPLVLK
     LLESTQGKGV VLAETKKAAE SVISAFQGLK ADFLVQSFVK EAAGEDIRCL VVGGKVVAAM
     RRRGKPDDFR SNLHQGGTAE PVRISKHERE AAIKAARAMR LDLAGVDLLR GADGPKVLEV
     NSSPGLEGIE RVSRKDIAGL IVAHIEAKVA PRPPRPRSRT RRDPPEASGL AAEAPEM
//