ID F0RFN3_CELLC Unreviewed; 463 AA.
AC F0RFN3;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Alpha-L-glutamate ligase, RimK family {ECO:0000313|EMBL:ADY28981.1};
GN OrderedLocusNames=Celly_1153 {ECO:0000313|EMBL:ADY28981.1};
OS Cellulophaga lytica (strain ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 /
OS NCIMB 1423 / VKM B-1433 / Cy l20).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cellulophaga.
OX NCBI_TaxID=867900 {ECO:0000313|EMBL:ADY28981.1, ECO:0000313|Proteomes:UP000007487};
RN [1] {ECO:0000313|EMBL:ADY28981.1, ECO:0000313|Proteomes:UP000007487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 / NCIMB 1423 /
RC VKM B-1433 / Cy l20 {ECO:0000313|Proteomes:UP000007487};
RX PubMed=21677859; DOI=10.4056/sigs.1774329;
RA Pati A., Abt B., Teshima H., Nolan M., Lapidus A., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Pagani I., Mavromatis K., Ovchinikova G., Chen A.,
RA Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA Brambilla E.M., Kannan K.P., Rohde M., Spring S., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Ivanova N.;
RT "Complete genome sequence of Cellulophaga lytica type strain (LIM- 21).";
RL Stand. Genomic Sci. 4:221-232(2011).
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DR EMBL; CP002534; ADY28981.1; -; Genomic_DNA.
DR RefSeq; WP_013620729.1; NC_015167.1.
DR AlphaFoldDB; F0RFN3; -.
DR STRING; 867900.Celly_1153; -.
DR KEGG; cly:Celly_1153; -.
DR eggNOG; COG0189; Bacteria.
DR eggNOG; COG4067; Bacteria.
DR HOGENOM; CLU_045509_1_0_10; -.
DR OrthoDB; 3865600at2; -.
DR Proteomes; UP000007487; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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 Ligase {ECO:0000313|EMBL:ADY28981.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000007487}.
FT DOMAIN 272..455
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 463 AA; 51168 MW; 9F1C78AF8A407132 CRC64;
MGNTTKFDEL QVIGGEEWCV FEELGIPAIK ARVDSGAKTS SIQANNVKVY NKGVEEWVKF
EVNPIQENRS VTITCEAPLV DRRTVKSSVG ISEERLVVKT SIKLGNNIHS VELTLANRDT
MEYRMLLGRE AINQRYIVNP AESYCMQNFS EEEIQEKYAS HMAEKSGLTI ALLASNPNLY
SNKRIIEAGE ARGHEVVFLN VENAYMKLDT KSPQIRYRGG NVLNKFDAVI PRIKPSVTFY
GCALIRQFDN LGVYCLNTAE AITQSRDKLF ASQLFSKNDI DIPITGFAKS PMDTKDLIRM
VNGAPLIIKL LESTQGKGVV LAETNKAAES VINAFKSVQT NILVQEFIKE ANGQDIRCFV
VNGKVVASMQ RQAQKGEFRA NIHQGGVASL IKITSEERKL AVKAAKILNL AVAGVDIIRS
NKGPLLLEVN SSPGLEGIEY ATGLDIANVM IRAIEKKLNY TSN
//
