ID A0A101CNR4_9FLAO Unreviewed; 456 AA.
AC A0A101CNR4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Alpha-L-glutamate ligase {ECO:0000313|EMBL:KUJ59584.1};
GN ORFNames=AR687_22450 {ECO:0000313|EMBL:KUJ59584.1};
OS Flavobacteriaceae bacterium CRH.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1742859 {ECO:0000313|EMBL:KUJ59584.1, ECO:0000313|Proteomes:UP000053826};
RN [1] {ECO:0000313|EMBL:KUJ59584.1, ECO:0000313|Proteomes:UP000053826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRH {ECO:0000313|EMBL:KUJ59584.1,
RC ECO:0000313|Proteomes:UP000053826};
RA Newman J.D., Miller J.R., Jacobs K.T.;
RT "Genome Sequence of Flavobacterium sp. CHR.";
RL Submitted (OCT-2015) 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:KUJ59584.1}.
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DR EMBL; LMAJ01000031; KUJ59584.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101CNR4; -.
DR STRING; 1742859.AR687_22450; -.
DR OrthoDB; 3865600at2; -.
DR Proteomes; UP000053826; 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:KUJ59584.1};
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}.
FT DOMAIN 267..450
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 456 AA; 50301 MW; 3B0CFFE169F4D2B7 CRC64;
MLQNKVILGS EEWCSFPELG IPTIKARVDS GAKTSAMHAI NIAPFIKNDA NWVKFDINPI
QNNTKTIIHC EAPLVDKRIV KSSSGFREHR YVIQTNLKIG DTKWPIEMTL TNRDSMGFRM
LLGREAMSGR VLVDPEEKYL LGQPSTETLK ELYQNSEKAT SGLRIGLLAS NPELYSNKRI
MEAGEMRGHE MHFLNIKECY MKLDAKTPEI HYRGGKILNQ FDAIIPRIRP SITFYGCALT
RQFEALKVYC LNSATAITQS RDKLYSLQLL LNSGIDIPTT GFANSPLDTD NLIKMVGGSP
LIVKLLEGTQ GKGVVLAETK KAAESVINAF KSLNANILVQ EFIKEANGKD IRCFVIDGKV
VAAIQREAMP GEFRANIHLG GTASVIKVTP EEKKIAIKAA KAMDLKVAGV DIIRSSKGPL
LLEVNSSPGL EGIEGATNKD IAGEMIRAIE KNFKLI
//
