DER_SALTY
ID DER_SALTY Reviewed; 490 AA.
AC Q9XCI8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=GTPase Der {ECO:0000255|HAMAP-Rule:MF_00195};
DE AltName: Full=GTP-binding protein EngA {ECO:0000255|HAMAP-Rule:MF_00195};
GN Name=der {ECO:0000255|HAMAP-Rule:MF_00195}; Synonyms=engA;
GN OrderedLocusNames=STM2519;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 223-490.
RC STRAIN=ATCC 14028 / SGSG 2980 / CDC 6516-60 / NCTC 12023;
RA Kingsley R.A., van Amsterdam K., Edwards E.W., Hargis B.M., Baumler A.J.;
RT "Complete sequence of the xseA-hisS intergenic region of the S. enterica
RT serotype Typhimurium genome and its distribution within the genus
RT Salmonella.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH S7, AND GDP- AND
RP GTP-BINDING.
RC STRAIN=FIRN / SL3261;
RX PubMed=17905831; DOI=10.1110/ps.072900907;
RA Lamb H.K., Thompson P., Elliott C., Charles I.G., Richards J., Lockyer M.,
RA Watkins N., Nichols C., Stammers D.K., Bagshaw C.R., Cooper A.,
RA Hawkins A.R.;
RT "Functional analysis of the GTPases EngA and YhbZ encoded by Salmonella
RT typhimurium.";
RL Protein Sci. 16:2391-2402(2007).
CC -!- FUNCTION: GTPase that plays an essential role in the late steps of
CC ribosome biogenesis. {ECO:0000255|HAMAP-Rule:MF_00195}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12.7 uM for GTP, high affinity site {ECO:0000269|PubMed:17905831};
CC KM=0.6 uM for GDP, high affinity site {ECO:0000269|PubMed:17905831};
CC KM=3.2 uM for GDP, low affinity site {ECO:0000269|PubMed:17905831};
CC Note=KM for GTP in the low affinity site could not be measured,
CC experiments performed in the absence of Mg(2+).;
CC -!- SUBUNIT: Associates with the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00195}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. EngA (Der) GTPase family. {ECO:0000255|HAMAP-
CC Rule:MF_00195}.
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DR EMBL; AE006468; AAL21413.1; -; Genomic_DNA.
DR EMBL; AF140550; AAD25116.1; -; Genomic_DNA.
DR RefSeq; NP_461454.1; NC_003197.2.
DR RefSeq; WP_000249411.1; NC_003197.2.
DR AlphaFoldDB; Q9XCI8; -.
DR SMR; Q9XCI8; -.
DR STRING; 99287.STM2519; -.
DR PaxDb; Q9XCI8; -.
DR EnsemblBacteria; AAL21413; AAL21413; STM2519.
DR GeneID; 1254041; -.
DR KEGG; stm:STM2519; -.
DR PATRIC; fig|99287.12.peg.2656; -.
DR HOGENOM; CLU_016077_6_2_6; -.
DR OMA; KFRFLEY; -.
DR PhylomeDB; Q9XCI8; -.
DR BioCyc; SENT99287:STM2519-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR Gene3D; 3.30.300.20; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00195; GTPase_Der; 1.
DR InterPro; IPR031166; G_ENGA.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR016484; GTP-bd_EngA.
DR InterPro; IPR032859; KH_dom-like.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR Pfam; PF14714; KH_dom-like; 1.
DR Pfam; PF01926; MMR_HSR1; 2.
DR PIRSF; PIRSF006485; GTP-binding_EngA; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR03594; GTPase_EngA; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 2.
DR PROSITE; PS51712; G_ENGA; 2.
PE 1: Evidence at protein level;
KW GTP-binding; Nucleotide-binding; Reference proteome; Repeat;
KW Ribosome biogenesis.
FT CHAIN 1..490
FT /note="GTPase Der"
FT /id="PRO_0000179040"
FT DOMAIN 3..166
FT /note="EngA-type G 1"
FT DOMAIN 203..376
FT /note="EngA-type G 2"
FT DOMAIN 377..461
FT /note="KH-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 9..16
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 56..60
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 118..121
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 209..216
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 256..260
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 321..324
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT CONFLICT 223..228
FT /note="LGEERV -> SVKKRL (in Ref. 2; AAD25116)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 490 AA; 54972 MW; 077781680E0AEF0F CRC64;
MVPVVALVGR PNVGKSTLFN RLTRTRDALV ADFPGLTRDR KYGRAEVEGR EFICIDTGGI
DGTEDGVETR MAEQSLLAIE EADVVLFMVD ARAGLMPADE AIAKHLRSRE KPTFLVANKT
DGLDPDQAVV DFYSLGLGEI YPIAASHGRG VLSLLEHVLL PWMDDVAPQE EVDEDAEYWA
QFEAEQNGEE APEDDFDPQS LPIKLAIVGR PNVGKSTLTN RILGEERVVV YDMPGTTRDS
IYIPMERDER EYVLIDTAGV RKRGKITDAV EKFSVIKTLQ AIEDANVVLL VIDAREGISD
QDLSLLGFIL NSGRSLVIVV NKWDGLSQEV KEQVKETLDF RLGFIDFARV HFISALHGSG
VGNLFESVRE AYDSSTRRVS TAMLTRIMTM AVEDHQPPLV RGRRVKLKYA HAGGYNPPIV
VIHGNQVKDL PDSYKRYLMN YFRKSLEVMG TPIRIQFKEG ENPYANKRNT LTPTQMRKRK
RLMKHIKKSK
