ID   Y443_BORPD              Reviewed;         290 AA.
AC   A9I0N5;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Nucleotide-binding protein Bpet0443 {ECO:0000255|HAMAP-Rule:MF_00636};
GN   OrderedLocusNames=Bpet0443;
OS   Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=340100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448;
RX   PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA   Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H.,
RA   Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA   Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA   Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA   Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T.,
RA   Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA   Martinez-Arias R.;
RT   "The missing link: Bordetella petrii is endowed with both the metabolic
RT   versatility of environmental bacteria and virulence traits of pathogenic
RT   Bordetellae.";
RL   BMC Genomics 9:449-449(2008).
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   -!- SEQUENCE CAUTION:
CC       Sequence=CAP40775.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AM902716; CAP40775.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A9I0N5; -.
DR   SMR; A9I0N5; -.
DR   STRING; 94624.Bpet0443; -.
DR   EnsemblBacteria; CAP40775; CAP40775; Bpet0443.
DR   KEGG; bpt:Bpet0443; -.
DR   eggNOG; COG1660; Bacteria.
DR   Proteomes; UP000001225; 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..290
FT                   /note="Nucleotide-binding protein Bpet0443"
FT                   /id="PRO_0000383220"
FT   BINDING         9..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00636"
FT   BINDING         58..61
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00636"
SQ   SEQUENCE   290 AA;  32426 MW;  D9B3A56C7EB1C83F CRC64;
     MLKVVLITGI SGSGKSVALR MLEDAGYTCI DNLPVRFLSE FVAGARDDGL ERVAIAIDVR
     SPGELAELPG VITAMRAMGT SLRVVFLDAN THTLAQRYSE SRRRHPLTDR LSRGGQTPSL
     LDCIALERDL LAPLRDQEHV IDTSDLTPGQ LRAWIRDLVQ ADRPPLVLTF ESFAYKRGVP
     SDADLVFDVR CLPNPYYDRT LRPLTGRDEP VATWLAGFEI VGQMIDDIAG YLRRWLPQYT
     QDTRNYLTVA IGCTGGQHRS VYVVEQLALR FAEHDPLLVR HRTQLPDEST