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Database: UniProt
Entry: A9E5T4_9FLAO
LinkDB: A9E5T4_9FLAO
Original site: A9E5T4_9FLAO 
ID   A9E5T4_9FLAO            Unreviewed;       459 AA.
AC   A9E5T4;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   24-JAN-2024, entry version 69.
DE   SubName: Full=Possible ribosomal protein S6 modification protein {ECO:0000313|EMBL:EDP95218.1};
GN   ORFNames=KAOT1_07032 {ECO:0000313|EMBL:EDP95218.1};
OS   Kordia algicida OT-1.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Kordia.
OX   NCBI_TaxID=391587 {ECO:0000313|EMBL:EDP95218.1, ECO:0000313|Proteomes:UP000002945};
RN   [1] {ECO:0000313|EMBL:EDP95218.1, ECO:0000313|Proteomes:UP000002945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OT-1 {ECO:0000313|EMBL:EDP95218.1,
RC   ECO:0000313|Proteomes:UP000002945};
RX   PubMed=21622754; DOI=10.1128/JB.05241-11;
RA   Lee H.S., Kang S.G., Kwon K.K., Lee J.H., Kim S.J.;
RT   "Genome sequence of the algicidal bacterium Kordia algicida OT-1.";
RL   J. Bacteriol. 193:4031-4032(2011).
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:EDP95218.1}.
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DR   EMBL; ABIB01000010; EDP95218.1; -; Genomic_DNA.
DR   RefSeq; WP_007093974.1; NZ_DS544873.1.
DR   AlphaFoldDB; A9E5T4; -.
DR   STRING; 391587.KAOT1_07032; -.
DR   eggNOG; COG0189; Bacteria.
DR   eggNOG; COG4067; Bacteria.
DR   HOGENOM; CLU_045509_1_0_10; -.
DR   OrthoDB; 3865600at2; -.
DR   Proteomes; UP000002945; 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:UP000002945}.
FT   DOMAIN          268..451
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   459 AA;  50788 MW;  B42092F5F11B9F13 CRC64;
     MNETTLKIIG SEEWCAFNAL KIPAVKARVD SGAKTSSIQA NNIKLIQKGN EEWISFEVNP
     IQENRSIVVK CEAKIFDKRM VKSSSGISEE RFVIKTPVTI GEDTFEIELT LANRDAMEFR
     MLLGREALMN RYVINPSKAL MEQNFSVTDI QEKYKHLIKE KSGLKIAVLA SNPNLFSNKR
     IMEAGIARGH EMVFLNVEQA YMKFDAKEPQ IRYRGGNIVG IFDAIVPRIK PSVTFYACAL
     IRQFDAMGAY CLNSAEAITQ SRDKLLATQL FAKHDLRIPI TGFANSPLDT KDLIKMVNGA
     PLIIKLLEST QGKGVVLAET TKAAESVINA FKSVKTNILV QEFIKEANGQ DIRCFVVNGK
     VVASMQRQAA KGEFRANIHQ GGKASKIKIT SEERKLAIKA AKILDLPVAG VDIIRSNKGP
     LLLEVNSSPG LEGIEGATGL DIANIMIEAI EKKLKFKRN
//
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