UREG_MYCTU
ID UREG_MYCTU Reviewed; 224 AA.
AC P9WFE3; L0T828; P0A664; P50051;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Urease accessory protein UreG {ECO:0000255|HAMAP-Rule:MF_01389};
GN Name=ureG {ECO:0000255|HAMAP-Rule:MF_01389}; OrderedLocusNames=Rv1852;
GN ORFNames=MTCY359.21c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=7559354; DOI=10.1128/jb.177.19.5644-5652.1995;
RA Clemens D.L., Lee B.-Y., Horwitz M.A.;
RT "Purification, characterization, and genetic analysis of Mycobacterium
RT tuberculosis urease, a potentially critical determinant of host-pathogen
RT interaction.";
RL J. Bacteriol. 177:5644-5652(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [3]
RP PROTEIN SEQUENCE OF 171-186 AND 193-224, SUBUNIT, GTPASE ACTIVITY, POSSIBLE
RP DISULFIDE BOND, AND MODELING.
RX PubMed=17309280; DOI=10.1021/bi6024676;
RA Zambelli B., Musiani F., Savini M., Tucker P., Ciurli S.;
RT "Biochemical studies on Mycobacterium tuberculosis UreG and comparative
RT modeling reveal structural and functional conservation among the bacterial
RT UreG family.";
RL Biochemistry 46:3171-3182(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Facilitates the functional incorporation of the urease nickel
CC metallocenter. This process requires GTP hydrolysis, probably
CC effectuated by UreG. {ECO:0000255|HAMAP-Rule:MF_01389}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (Probable). The physiological role
CC of the disulfide bond has not been proven in vivo. UreD, UreF and UreG
CC form a complex that acts as a GTP-hydrolysis-dependent molecular
CC chaperone, activating the urease apoprotein by helping to assemble the
CC nickel containing metallocenter of UreC. The UreE protein probably
CC delivers the nickel (By similarity). {ECO:0000250, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01389}.
CC -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. UreG
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01389}.
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; U33011; AAC43477.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP44618.1; -; Genomic_DNA.
DR PIR; D70665; D70665.
DR RefSeq; NP_216368.1; NC_000962.3.
DR RefSeq; WP_003409313.1; NZ_NVQJ01000013.1.
DR AlphaFoldDB; P9WFE3; -.
DR SMR; P9WFE3; -.
DR STRING; 83332.Rv1852; -.
DR PaxDb; P9WFE3; -.
DR DNASU; 885729; -.
DR GeneID; 885729; -.
DR KEGG; mtu:Rv1852; -.
DR TubercuList; Rv1852; -.
DR eggNOG; COG0378; Bacteria.
DR OMA; VDLTIYV; -.
DR PhylomeDB; P9WFE3; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:MTBBASE.
DR GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01389; UreG; 1.
DR InterPro; IPR003495; CobW/HypB/UreG_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004400; UreG.
DR PANTHER; PTHR31715; PTHR31715; 1.
DR Pfam; PF02492; cobW; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00101; ureG; 1.
PE 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW GTP-binding; Nickel insertion; Nucleotide-binding; Reference proteome.
FT CHAIN 1..224
FT /note="Urease accessory protein UreG"
FT /id="PRO_0000067669"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32..39
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01389"
FT DISULFID 90
FT /note="Interchain"
FT /evidence="ECO:0000255"
SQ SEQUENCE 224 AA; 23348 MW; 702D613945D76BB9 CRC64;
MATHSHPHSH TVPARPRRVR KPGEPLRIGV GGPVGSGKTA LVAALCRQLR GELSLAVLTN
DIYTTEDADF LRTHAVLPDD RIAAVQTGGC PHTAIRDDIT ANLDAIDELM AAHDALDLIL
VESGGDNLTA TFSSGLVDAQ IFVIDVAGGD KVPRKGGPGV TYSDLLVVNK TDLAALVGAD
LAVMARDADA VRDGRPTVLQ SLTEDPAASD VVAWVRSQLA ADGV
