ID A0A1I5MM33_9RHOB Unreviewed; 473 AA.
AC A0A1I5MM33;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=SSU ribosomal protein S6P modification protein {ECO:0000313|EMBL:SFP10652.1};
GN ORFNames=SAMN04488047_102329 {ECO:0000313|EMBL:SFP10652.1};
OS Tranquillimonas alkanivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Tranquillimonas.
OX NCBI_TaxID=441119 {ECO:0000313|EMBL:SFP10652.1, ECO:0000313|Proteomes:UP000199356};
RN [1] {ECO:0000313|EMBL:SFP10652.1, ECO:0000313|Proteomes:UP000199356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19547 {ECO:0000313|EMBL:SFP10652.1,
RC ECO:0000313|Proteomes:UP000199356};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FOXA01000002; SFP10652.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5MM33; -.
DR STRING; 441119.SAMN04488047_102329; -.
DR OrthoDB; 3865600at2; -.
DR Proteomes; UP000199356; 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:UP000199356}.
FT DOMAIN 272..455
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 473 AA; 51493 MW; 9F2BA6F9175F2321 CRC64;
MADDATPQDT AFRLGWEEWV SLPDLGLPAL KAKVDTGART SALHAYEIEP FGPAARPRVR
FMVHPVPGRS DLAIPCSAEV LDRREVTSSN GETELRYVIQ SEISVGGRTW PIELTLTDRG
TMAYRMLLGR QALSEDIVVS PGDSFCQPSL TYDVYHSTRV REVAPDRTLR IAVLSREGHS
YSTRRLVAEG EKRGHVVEVI DTTRCYMTIN SLAPEVHYDG KRLPRYDAVI PRIGASITPY
GTAVIRQFET IGTYCVNGSE GIAASRDKLQ AHQVLARHRI GMPTTAFAAS PKDTGNLIQL
VGAAPLIVKL LESTQGKGVV LAETKKAAES VISAFRGLKA NFLVQQFVKE AAGEDIRCLV
MNGRVVASIR RVAQPGEFRS NLHQGGVAEA VRLTKAERET ALRAAKAFRL GLAGVDLLRS
SDGPKVLEVN SSPGLEGIEK ATGKNVAGSL YEAIEKHVRP EPVRRRAARR TAG
//