ID Q7W213_BORPA Unreviewed; 369 AA.
AC Q7W213;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 24-JAN-2024, entry version 85.
DE RecName: Full=CobW C-terminal domain-containing protein {ECO:0000259|SMART:SM00833};
GN OrderedLocusNames=BPP0179 {ECO:0000313|EMBL:CAE39920.1};
OS Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257311 {ECO:0000313|EMBL:CAE39920.1, ECO:0000313|Proteomes:UP000001421};
RN [1] {ECO:0000313|Proteomes:UP000001421}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12822 / ATCC BAA-587 / NCTC 13253
RC {ECO:0000313|Proteomes:UP000001421};
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
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; BX640423; CAE39920.1; -; Genomic_DNA.
DR RefSeq; WP_010927333.1; NC_002928.3.
DR AlphaFoldDB; Q7W213; -.
DR GeneID; 69419563; -.
DR KEGG; bpa:BPP0179; -.
DR HOGENOM; CLU_017452_0_0_4; -.
DR OMA; QEEFFPV; -.
DR Proteomes; UP000001421; Chromosome.
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:SF69; 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}.
FT DOMAIN 273..367
FT /note="CobW C-terminal"
FT /evidence="ECO:0000259|SMART:SM00833"
FT REGION 229..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 369 AA; 41379 MW; E9AB11BF2B3B9C3A CRC64;
MNTARSLDKM VPVTILTGFL GAGKTTLLKR ILTEYHGRRV AVIENEFGPE SIDNDLLVQD
RDEEIIELSN GCVCCTVRGD LMRTLSDLRA RREAGELSFE RVIIETTGMA NPGPVCQTFF
MDDDIAEYYR LDAVVTVVDA KHGMATLDAQ DEAQKQVGFA DRILVSKKDL VNDVDYAALH
QRLVRINPRA PITPVHFGEA DLKSIIDISG FNLNSILDID PAFLADEHPD AAHDHHDHDH
GHSHEHDHDH EGECGAHCNH HHHHHHAHHD DEIGAFVFRS NKPFDPARLE EFLGGVVQVY
GPDLLRYKGI LYMKGINRRM LFQGVHMMMG AEPGKAWTAA EKPSTKMVFI GRKLPQEIFT
RGLEQCLVG
//