ID A4A975_9GAMM Unreviewed; 462 AA.
AC A4A975;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE SubName: Full=SSU ribosomal protein S6P modification protein {ECO:0000313|EMBL:EAQ97617.1};
GN ORFNames=KT71_04890 {ECO:0000313|EMBL:EAQ97617.1};
OS Congregibacter litoralis KT71.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Congregibacter.
OX NCBI_TaxID=314285 {ECO:0000313|EMBL:EAQ97617.1, ECO:0000313|Proteomes:UP000019205};
RN [1] {ECO:0000313|EMBL:EAQ97617.1, ECO:0000313|Proteomes:UP000019205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT71 {ECO:0000313|EMBL:EAQ97617.1,
RC ECO:0000313|Proteomes:UP000019205};
RX PubMed=17299055; DOI=10.1073/pnas.0608046104;
RA Fuchs B.M., Spring S., Teeling H., Quast C., Wulf J., Schattenhofer M.,
RA Yan S., Ferriera S., Johnson J., Glockner F.O., Amann R.;
RT "Characterization of a marine gammaproteobacterium capable of aerobic
RT anoxygenic photosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2891-2896(2007).
RN [2] {ECO:0000313|EMBL:EAQ97617.1, ECO:0000313|Proteomes:UP000019205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT71 {ECO:0000313|EMBL:EAQ97617.1,
RC ECO:0000313|Proteomes:UP000019205};
RX PubMed=19287491; DOI=10.1371/journal.pone.0004866;
RA Spring S., Lunsdorf H., Fuchs B.M., Tindall B.J.;
RT "The photosynthetic apparatus and its regulation in the aerobic
RT gammaproteobacterium Congregibacter litoralis gen. nov., sp. nov.";
RL PLoS ONE 4:E4866-E4866(2009).
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:EAQ97617.1}.
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DR EMBL; AAOA02000002; EAQ97617.1; -; Genomic_DNA.
DR AlphaFoldDB; A4A975; -.
DR STRING; 314285.KT71_04890; -.
DR eggNOG; COG0189; Bacteria.
DR eggNOG; COG4067; Bacteria.
DR HOGENOM; CLU_045509_1_1_6; -.
DR OrthoDB; 3865600at2; -.
DR Proteomes; UP000019205; 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 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:UP000019205}.
FT DOMAIN 268..451
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 462 AA; 50549 MW; EEBD08FF7771E381 CRC64;
MNQDQKLIVG SEEWCSFPAL GIPAVKARVD SGAKTSSLHA FNIHPFNRNG EKWISFEVHP
IQRNRKTTVR CESPVIDRRF VKSSSGDREK RYVINSSVHI GGSSFDIELT LSNRDTMGYR
MLLGREAMSG RMLVDPAASF SVGDLTPTQL SQMYGVATEP SSGLKIGVLA SNPELYSNKR
LMEAGANRGH EMVFLDIKLC YMKLDAETPE IHYRGGWILN DIDAVIPRIR PQLTFYGCAL
TRHFESIDVY PLNNASSISY SRDKLYSLQL LQRKGLEIPT TGFANSPMDT AELIDMVGGA
PLIVKLLQGT QGRGVVLAET RKAGESVINA IKSLNANLLV QEFIKEAQGR DLRCFVIDGK
VIASIERRAA PGEFRANLHQ GGSAALVRIT PEERRLAIKA TKALGLQVAG VDIIRSAKGP
LLLEVNSSPG LEGIETATGK DIAGDMIASI ERALNWKPAA KT
//
