ID Q88IP3_PSEPK Unreviewed; 526 AA.
AC Q88IP3;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE SubName: Full=Ribosomal protein S6 modification protein-related protein {ECO:0000313|EMBL:AAN68564.1};
GN OrderedLocusNames=PP_2956 {ECO:0000313|EMBL:AAN68564.1};
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488 {ECO:0000313|EMBL:AAN68564.1, ECO:0000313|Proteomes:UP000000556};
RN [1] {ECO:0000313|EMBL:AAN68564.1, ECO:0000313|Proteomes:UP000000556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440
RC {ECO:0000313|Proteomes:UP000000556};
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L., Beanan M., DeBoy R.T., Daugherty S., Kolonay J., Madupu R.,
RA Nelson W., White O., Peterson J., Khouri H., Hance I., Chris Lee P.,
RA Holtzapple E., Scanlan D., Tran K., Moazzez A., Utterback T., Rizzo M.,
RA Lee K., Kosack D., Moestl D., Wedler H., Lauber J., Stjepandic D.,
RA Hoheisel J., Straetz M., Heim S., Kiewitz C., Eisen J.A., Timmis K.N.,
RA Dusterhoft A., Tummler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
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DR EMBL; AE015451; AAN68564.1; -; Genomic_DNA.
DR RefSeq; NP_745100.1; NC_002947.4.
DR RefSeq; WP_010953856.1; NC_002947.4.
DR AlphaFoldDB; Q88IP3; -.
DR STRING; 160488.PP_2956; -.
DR PaxDb; 160488-PP_2956; -.
DR GeneID; 83680458; -.
DR KEGG; ppu:PP_2956; -.
DR PATRIC; fig|160488.4.peg.3130; -.
DR eggNOG; COG0189; Bacteria.
DR HOGENOM; CLU_016765_0_0_6; -.
DR OrthoDB; 9800957at2; -.
DR PhylomeDB; Q88IP3; -.
DR BioCyc; PPUT160488:G1G01-3137-MONOMER; -.
DR Proteomes; UP000000556; Chromosome.
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 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; IPR025839; RLAN_dom.
DR PANTHER; PTHR21621:SF0; BETA-CITRYLGLUTAMATE SYNTHASE B-RELATED; 1.
DR PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR Pfam; PF08443; RimK; 1.
DR Pfam; PF14401; RLAN; 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:UP000000556}.
FT DOMAIN 321..514
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 526 AA; 59319 MW; AEE0307686CF5C7B CRC64;
MSAVQANVAE VLAKTEVSTI TLSEEPPSKR SAGNRLLIVV ERKEDWASYF PSESLMLAQD
YIEHSDDVAR RTQVINLCRS YKYLGQGYYC SLLAEARGHK VFPSVRTISE LTRKALYGVG
LDDLERTLER ALADHPYGST EAFTLTLYFG RTAIEPLQDI GRQLFESFPC PVLLVEFRRR
DTWQIDGIKA GALHKLRDEQ QYLFANALDA FNRRTWRQPA SKRLARFDLA ILHDPAEALP
PSNPEALEQF IENGKQLGID VELIEKKDYA RLAEFDALFI RETTRVDDHT YRFAKKAESE
GLVVIDDPSS ILRCTNKVYL ADLLKRHNLG APATEILYKD RPQELELVGR RLGFPLVLKI
PDGCFSKGVI KVADAQALAS AAQELFEHSV LLLAQEYCYT EYDWRIGVLN GEALYACQYF
MSKGHWQIYN HKAQAGEVNG LCRAVPVEQA PPEVVKLAVD TARLIGQGLY GVDLKQTGDR
VLVIEVNDNP NLDAGTEDAV LGNALYQRVL QAFVQRLERK HLGQAW
//
