ID   Y1710_COREF             Reviewed;         314 AA.
AC   Q8FT61;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Nucleotide-binding protein CE1710 {ECO:0000255|HAMAP-Rule:MF_00636};
GN   OrderedLocusNames=CE1710;
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS   / NBRC 100395).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA   Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(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-43 (instead of
CC       a conserved basic residue). {ECO:0000305}.
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DR   EMBL; BA000035; BAC18520.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8FT61; -.
DR   SMR; Q8FT61; -.
DR   STRING; 196164.23493550; -.
DR   EnsemblBacteria; BAC18520; BAC18520; BAC18520.
DR   KEGG; cef:CE1710; -.
DR   eggNOG; COG1660; Bacteria.
DR   HOGENOM; CLU_059558_0_0_11; -.
DR   OMA; TVMSFGF; -.
DR   Proteomes; UP000001409; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; -; 1.
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..314
FT                   /note="Nucleotide-binding protein CE1710"
FT                   /id="PRO_0000107701"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         37..44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00636"
FT   BINDING         88..91
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00636"
SQ   SEQUENCE   314 AA;  34951 MW;  18A65225E5E45560 CRC64;
     MNQTPGSTVP ETATPVTSPA SSPSAPETTF TPVIITGMSG AGLSTAARVL EDLGWFVTHN
     LPPQMILPLV EMCAREDSPV DKVAVVCDVR SREFRGGLRE TITELEEKNL APTVLFLDAR
     DDELIRRFDN VRRTHPLQGS QTLQVGIERE RQMLSDLKEE ADVVIDTSEL SVHDLRRAIE
     SSFRTIAKRV QHVTIESFGF KHGSPRDADF IIDARFLPNP FWVPELRPFR GVDKPVSDYV
     LSQKGAGEFL DNFIAMLDDM LPGYRHEGKN FITVGIGCTG GHHRSVAVSE ELARRLGERP
     DLDVSVVHRD INRN