ID A0A1M4ZGK7_9FLAO Unreviewed; 454 AA.
AC A0A1M4ZGK7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=SSU ribosomal protein S6P modification protein {ECO:0000313|EMBL:SHF17170.1};
GN ORFNames=SAMN05444377_104177 {ECO:0000313|EMBL:SHF17170.1};
OS Flavobacterium fontis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1124188 {ECO:0000313|EMBL:SHF17170.1, ECO:0000313|Proteomes:UP000184147};
RN [1] {ECO:0000313|EMBL:SHF17170.1, ECO:0000313|Proteomes:UP000184147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25660 {ECO:0000313|EMBL:SHF17170.1,
RC ECO:0000313|Proteomes:UP000184147};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FQVQ01000004; SHF17170.1; -; Genomic_DNA.
DR RefSeq; WP_073362381.1; NZ_FQVQ01000004.1.
DR AlphaFoldDB; A0A1M4ZGK7; -.
DR STRING; 1124188.SAMN05444377_104177; -.
DR OrthoDB; 3865600at2; -.
DR Proteomes; UP000184147; 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:UP000184147}.
FT DOMAIN 265..448
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 454 AA; 50289 MW; 483411A2F4287007 CRC64;
MQKLILGSEE WCGFPQLGLP TIKARVDSGA KTSALHAVNI APFQKEGETW VKFDINPIQK
NQKTIIHCEA KVVDKRVVKS SSGYREQRYV IQTDLQLGDE CWSVEVTLTN RDSMGFRMLL
GREAMSGRIL VDPEQKYLLG EPTTEYLKEV YQKAVAQRTG LRIGLLASNP ELYSNRRIME
AGEARGHEMH FLNIKECYMK LDAVKPEIHY RGGKILDNFD AIIPRIRPSI TFYGCALTRQ
FEAMKVYCLN SAKAITQSRD KLYSLQLLLH HGVDIPTTGF ANSPLDTDDL IKMVGGTPLI
VKLLEGTQGK GVVLAETKKA AESVINAFKS LNANILVQEF IKEADGKDLR LFVVDGKVVA
AMQREAAPGE FRANIHMGGT ASVVKVTPEE KRIAIKAAKA MDLKVAGVDI IRSSKGPLLL
EVNSSPGLEG IEGATNKDIA GEMIKSIEKN FKWK
//
