ID Q63YI1_BURPS Unreviewed; 370 AA.
AC Q63YI1;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=CobW C-terminal domain-containing protein {ECO:0000259|SMART:SM00833};
GN OrderedLocusNames=BPSL0206 {ECO:0000313|EMBL:CAH34193.1};
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH34193.1, ECO:0000313|Proteomes:UP000000605};
RN [1] {ECO:0000313|EMBL:CAH34193.1, ECO:0000313|Proteomes:UP000000605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243 {ECO:0000313|EMBL:CAH34193.1,
RC ECO:0000313|Proteomes:UP000000605};
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.M., Atkins T.,
RA Crossman L.C., Pitt T., Churcher C., Mungall K., Bentley S.D., Sebaihia M.,
RA Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F.,
RA Challis G.L., Cherevach I., Chillingworth T., Cronin A., Crosset B.,
RA Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H.,
RA Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M.,
RA Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S.,
RA Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. ZNG1
CC subfamily. {ECO:0000256|ARBA:ARBA00034320}.
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DR EMBL; BX571965; CAH34193.1; -; Genomic_DNA.
DR RefSeq; YP_106834.1; NC_006350.1.
DR AlphaFoldDB; Q63YI1; -.
DR STRING; 272560.BPSL0206; -.
DR KEGG; bps:BPSL0206; -.
DR PATRIC; fig|272560.6.peg.219; -.
DR eggNOG; COG0523; Bacteria.
DR Proteomes; UP000000605; Chromosome 1.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd03112; CobW-like; 1.
DR Gene3D; 3.30.1220.10; CobW-like, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR036627; CobW-likC_sf.
DR InterPro; IPR011629; CobW-like_C.
DR InterPro; IPR003495; CobW/HypB/UreG_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13748:SF62; COBW DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR13748; COBW-RELATED; 1.
DR Pfam; PF02492; cobW; 1.
DR Pfam; PF07683; CobW_C; 1.
DR SMART; SM00833; CobW_C; 1.
DR SUPFAM; SSF90002; Hypothetical protein YjiA, C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000000605}.
FT DOMAIN 275..369
FT /note="CobW C-terminal"
FT /evidence="ECO:0000259|SMART:SM00833"
FT REGION 236..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 370 AA; 41579 MW; 331BDEB7EDE69C15 CRC64;
MTPFHEPQAT DDMAIPVTIL TGFLGSGKTT LLKRILNEQH GMKIAVIENE FGEENIDNEI
LVQDSTEQII QMSNGCICCT IRGDLARALA DLAAKKRDGT FDFDRVVIET TGLANPGPVA
QTFFIDSEIA DEFLLDAVIT LVDAKHANAQ LDEHEVVQRQ VGFADRLFIT KADLVDDEAV
SELKHRLLHM NPKAAIKVVN FGDADIKEIF DLRGFNLNAK LEIDPDFLAE DDHAHAHHDD
HDHDHAHCDH DHGHCEHDHG HGHHDHHHAH HDDKIKSFVY RNDRPFDPNK LEDFLGGILQ
IYGERMLRYK GVLYMKGVDR KVVFQGVHQM MGSDLAAKWL PAEKKTNKMV FIGVDLPRDL
ITDGLDACLA
//
