ID A0A2S8XVA4_9PSED Unreviewed; 350 AA.
AC A0A2S8XVA4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=GTP-binding protein {ECO:0000313|EMBL:PRA41496.1};
GN ORFNames=CQZ98_28025 {ECO:0000313|EMBL:PRA41496.1};
OS Pseudomonas sp. MYb115.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1848717 {ECO:0000313|EMBL:PRA41496.1, ECO:0000313|Proteomes:UP000239970};
RN [1] {ECO:0000313|EMBL:PRA41496.1, ECO:0000313|Proteomes:UP000239970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MYb115 {ECO:0000313|EMBL:PRA41496.1,
RC ECO:0000313|Proteomes:UP000239970};
RA Zimmermann J., Obeng N., Yang W., Obeng O., Kissoyan K., Pees B.,
RA Dirksen P., Hoppner M., Franke A., Rosenstiel P., Leippe M., Dierking K.,
RA Kaleta C., Schulenburg H.;
RT "Genomic, metabolic, and phenotypic characteristics of bacterial isolates
RT from the natural microbiome of the model nematode Caenorhabditis elegans.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PRA41496.1}.
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DR EMBL; PCQM01000049; PRA41496.1; -; Genomic_DNA.
DR RefSeq; WP_027620753.1; NZ_PCQM01000049.1.
DR AlphaFoldDB; A0A2S8XVA4; -.
DR Proteomes; UP000239970; Unassembled WGS sequence.
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:SF59; COBW C-TERMINAL 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}.
FT DOMAIN 255..348
FT /note="CobW C-terminal"
FT /evidence="ECO:0000259|SMART:SM00833"
FT REGION 233..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 350 AA; 38575 MW; B796EF610D57CDB3 CRC64;
MTTPFNAPTP NRKIPVTILT GFLGAGKTTL LNYILKENHG RKIAVIENEF GEVGIDGDLV
LSSETEEIYE MVNGCVCCTA EVREDLVRIV RELVARPVRL DHILIETSGL ADPYPVAQSF
FINDPIAEEV ELDAIVTMVD AKHVAQHLED LQLDGVDNQA VDQIVCADRI VINKVDLVSE
AEVAALSAKI RGLNATAELV TSHYAQIDLS RILGVGAFES TQKLMEIGAE HEHHADDHRH
EHEHDELEHE HDPSVSSVGI SVDGAVNLGA FHRWISQLRN DQAETLYRMK GVLAVKDQDQ
RYVLQGVHSL VEFRASTLWG NEPRSSKIVF IGRDLDRAAL NQGFAACLAG
//
