ID A0A243SHA5_9FLAO Unreviewed; 460 AA.
AC A0A243SHA5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Alpha-L-glutamate ligase {ECO:0000313|EMBL:OUD36624.1};
GN ORFNames=FPG59_05350 {ECO:0000313|EMBL:OUD36624.1};
OS Flavobacterium sp. FPG59.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1929267 {ECO:0000313|EMBL:OUD36624.1, ECO:0000313|Proteomes:UP000195161};
RN [1] {ECO:0000313|EMBL:OUD36624.1, ECO:0000313|Proteomes:UP000195161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FPG59 {ECO:0000313|EMBL:OUD36624.1};
RA Wu A., Liu R., Kropinski A.M., Macinnes J.I.;
RT "The genome of Flavobacter psychrophilum strain FPG59.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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:OUD36624.1}.
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DR EMBL; MTCA01000034; OUD36624.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A243SHA5; -.
DR OrthoDB; 3865600at2; -.
DR Proteomes; UP000195161; Unassembled WGS sequence.
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 HAMAP; MF_01552; RimK; 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; IPR023533; RimK.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:OUD36624.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000195161}.
FT DOMAIN 267..450
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 460 AA; 50800 MW; DE982074D4A91BB4 CRC64;
MPDNKVILGS EEWCSFPELG IPTIKARVDS GAKTSALHAI NIAPFIKNDS NWVKFDINPI
QNNLKTVIHC EAPLIDKRIV KSSSGFREQR YVIQTNLQLG TAQWPIEMTL TNRDSMGFRM
LLGREAMSGR VLVDPEQKYL LGQPTTDTLK ELYKNSEKAA SGLRIGLLAS NPELYSNKRI
MEAGEMRGHE MHFLNIKECY MKLDAKTPEI HYRGGKILNQ FDAIIPRIRP SITFYGCALT
RQFEALKVYC LNSSNAITQS RDKLYSLQLL LNHGVEIPTT GFANSPLDTD DLIKMVGGSP
LIVKLLEGTQ GKGVVLAETK KAAESVINAF KSLNANILVQ EFIKEANGKD IRCFVIDGKV
VAAIQREAMP GEFRANIHLG GTASVIKVTP EEKKIAIKAT KAMDLKVAGV DIIRSSKGPL
LLEVNSSPGL EGIEGATNKD IAGEMIKAIE KHFHQKTDLK
//
