Y2483_CAUVC
ID Y2483_CAUVC Reviewed; 326 AA.
AC P37895;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Putative GTPase CC_2483;
DE EC=3.6.-.-;
GN OrderedLocusNames=CC_2483;
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=8421698; DOI=10.1073/pnas.90.2.630;
RA Wang S.P., Sharma P.L., Schoenlein P.V., Ely B.;
RT "A histidine protein kinase is involved in polar organelle development in
RT Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:630-634(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
CC -!- FUNCTION: May have GTPase activity. May also bind and hydrolyze ATP.
CC May function as chaperone (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. ArgK/MeaB
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M91449; AAA23053.1; -; Genomic_DNA.
DR EMBL; AE005673; AAK24454.1; -; Genomic_DNA.
DR PIR; B87557; B87557.
DR PIR; S27534; S27534.
DR RefSeq; NP_421286.1; NC_002696.2.
DR RefSeq; WP_010920341.1; NC_002696.2.
DR AlphaFoldDB; P37895; -.
DR SMR; P37895; -.
DR STRING; 190650.CC_2483; -.
DR EnsemblBacteria; AAK24454; AAK24454; CC_2483.
DR KEGG; ccr:CC_2483; -.
DR PATRIC; fig|190650.5.peg.2501; -.
DR eggNOG; COG1703; Bacteria.
DR HOGENOM; CLU_043725_1_1_5; -.
DR OMA; WMWERID; -.
DR BioCyc; CAULO:CC2483-MON; -.
DR Proteomes; UP000001816; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005129; GTPase_ArgK.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23408; PTHR23408; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00750; lao; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; GTP-binding; Hydrolase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..326
FT /note="Putative GTPase CC_2483"
FT /id="PRO_0000157820"
FT BINDING 61..69
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 238..240
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT CONFLICT 77
FT /note="N -> K (in Ref. 1; AAA23053)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 326 AA; 34551 MW; 3F58765201CEF32D CRC64;
MIPALDIDSL EHRLVAGDRA ALARAITLVE SRRADHQVAA RTLLSRLMPL TGRAQRIGIT
GVPGAGKSTT IERFGCNLVE AGHRVAVLAV DPSSGRHGGS ILGDKTRMEQ LSVQANAFIR
PSPSGGALGG VARKTREAML LCEAAGFDVV IIETVGVGQS ETVVADMVDI FLALLIPGGG
DELQGIKKGL IELADLLVIN KADADPAKAE RSARDYRNAL HILTPAHPDW TPPVLTASGL
TGQGLDVLWT QILRHREVMT ANGARAARRA DQDARWMWAM VRDRLEDAFK TAPAVAALVP
DLETAVREGE VPASAAADRL LAAFGL
