Y1591_CORGL
ID Y1591_CORGL Reviewed; 309 AA.
AC Q8NQ56;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Nucleotide-binding protein Cgl1591/cg1794 {ECO:0000255|HAMAP-Rule:MF_00636};
GN OrderedLocusNames=Cgl1591, cg1794;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
CC -!- FUNCTION: Displays ATPase and GTPase activities. {ECO:0000255|HAMAP-
CC Rule:MF_00636}.
CC -!- SIMILARITY: Belongs to the RapZ-like family. {ECO:0000255|HAMAP-
CC Rule:MF_00636}.
CC -!- CAUTION: Lacks the conserved ATP-binding site due to Leu-38 (instead of
CC a conserved basic residue). {ECO:0000305}.
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DR EMBL; BA000036; BAB98984.1; -; Genomic_DNA.
DR EMBL; BX927152; CAF21599.1; -; Genomic_DNA.
DR RefSeq; NP_600805.1; NC_003450.3.
DR RefSeq; WP_003856023.1; NC_006958.1.
DR AlphaFoldDB; Q8NQ56; -.
DR SMR; Q8NQ56; -.
DR STRING; 196627.cg1794; -.
DR GeneID; 58309224; -.
DR KEGG; cgb:cg1794; -.
DR KEGG; cgl:Cgl1591; -.
DR PATRIC; fig|196627.13.peg.1553; -.
DR eggNOG; COG1660; Bacteria.
DR HOGENOM; CLU_059558_0_0_11; -.
DR OMA; TVMSFGF; -.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00636; RapZ_like; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005337; RapZ-like.
DR PANTHER; PTHR30448; PTHR30448; 1.
DR Pfam; PF03668; ATP_bind_2; 1.
DR PIRSF; PIRSF005052; P-loopkin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW ATP-binding; GTP-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..309
FT /note="Nucleotide-binding protein Cgl1591/cg1794"
FT /id="PRO_0000107702"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00636"
FT BINDING 83..86
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00636"
SQ SEQUENCE 309 AA; 34710 MW; 0D77FD978C769695 CRC64;
MIQSTGVTHT DKSAQENPVK YRDNFTPVII TGMSGAGLST AARVLEDLGW YVAHNIPPQI
ILELIDMCAR EDSPVDKVAV VCDVRSREFR GSLTQVVSEL RDKQLDPTVL FLEARDEVLI
KRFDNVRRTH PLQGSQTLQV GIERERTVLS PVKEDASVVI DTSDLSVHDL RRAIESSFRT
IATRTQHVTI ESFGFKHGSP RDADFVVDVR FLPNPFWVPE LRPFRGVDKP VSDYVLSQKG
AEEFLNNFVD MLKDMLPGYR HEGKNFITIG VGCTGGHHRS VAVSEELAKR IADQTTLDVS
VVHRDINRH
