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Database: UniProt
Entry: A0A0M2H9J0_9MICO
LinkDB: A0A0M2H9J0_9MICO
Original site: A0A0M2H9J0_9MICO 
ID   A0A0M2H9J0_9MICO        Unreviewed;       510 AA.
AC   A0A0M2H9J0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=GTPase Der {ECO:0000256|ARBA:ARBA00020953, ECO:0000256|HAMAP-Rule:MF_00195};
DE   AltName: Full=GTP-binding protein EngA {ECO:0000256|HAMAP-Rule:MF_00195};
GN   Name=der {ECO:0000256|HAMAP-Rule:MF_00195,
GN   ECO:0000313|EMBL:KJL41300.1};
GN   ORFNames=RS81_01367 {ECO:0000313|EMBL:KJL41300.1};
OS   Microbacterium ketosireducens.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=92835 {ECO:0000313|EMBL:KJL41300.1, ECO:0000313|Proteomes:UP000033956};
RN   [1] {ECO:0000313|EMBL:KJL41300.1, ECO:0000313|Proteomes:UP000033956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12510 {ECO:0000313|EMBL:KJL41300.1,
RC   ECO:0000313|Proteomes:UP000033956};
RA   Corretto E.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT   metal contaminated environments.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: GTPase that plays an essential role in the late steps of
CC       ribosome biogenesis. {ECO:0000256|HAMAP-Rule:MF_00195,
CC       ECO:0000256|RuleBase:RU004481}.
CC   -!- SUBUNIT: Associates with the 50S ribosomal subunit. {ECO:0000256|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.
CC       {ECO:0000256|ARBA:ARBA00008279, ECO:0000256|HAMAP-Rule:MF_00195,
CC       ECO:0000256|PROSITE-ProRule:PRU01049, ECO:0000256|RuleBase:RU004481}.
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:KJL41300.1}.
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DR   EMBL; JYIZ01000044; KJL41300.1; -; Genomic_DNA.
DR   RefSeq; WP_045275327.1; NZ_JYIZ01000044.1.
DR   AlphaFoldDB; A0A0M2H9J0; -.
DR   STRING; 92835.RS81_01367; -.
DR   PATRIC; fig|92835.4.peg.1387; -.
DR   OrthoDB; 9805918at2; -.
DR   Proteomes; UP000033956; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR   CDD; cd01894; EngA1; 1.
DR   CDD; cd01895; EngA2; 1.
DR   Gene3D; 3.30.300.20; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   HAMAP; MF_00195; GTPase_Der; 1.
DR   InterPro; IPR031166; G_ENGA.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR016484; GTPase_Der.
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   NCBIfam; TIGR03594; GTPase_EngA; 1.
DR   NCBIfam; TIGR00231; small_GTP; 2.
DR   PANTHER; PTHR43834:SF6; GTP-BINDING PROTEIN ENGA; 1.
DR   PANTHER; PTHR43834; GTPASE DER; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51712; G_ENGA; 2.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00195};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00195}; Reference proteome {ECO:0000313|Proteomes:UP000033956};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU004481};
KW   Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517, ECO:0000256|HAMAP-
KW   Rule:MF_00195}.
FT   DOMAIN          70..233
FT                   /note="EngA-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51712"
FT   DOMAIN          244..423
FT                   /note="EngA-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51712"
FT   BINDING         76..83
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         123..127
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         185..188
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         250..257
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         297..301
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         362..365
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
SQ   SEQUENCE   510 AA;  56392 MW;  F06828213F2D07FD CRC64;
     MSSDTSAEEY EPGEDHLAEN LAAIDDELAD QRAAALRVGL EDYDLDDDDA ELLAGLIRGE
     DGIEYLPALP VVAIVGRPNV GKSALVNRIL GRREAVVEDT PGVTRDRVTY KAEWMDRRFS
     LVDTGGWEPD ARGIDKSVAL QAEVAIDLCD VVMFVVDAMV GATSTDEQVV KLLRKSGKPV
     FLVANKIDDA RHEPEAAALW NLGLGEPHPV SAIHGRGVAD LLDEIMKVLP EVSAVAQAEI
     GGPRRVAILG RPNVGKSSLL NKAAGEERVV VNELAGTTRD PVDEIVELGG KLWRFVDTAG
     IRRRVHLQQG ADFYASLRTS AALEKAEVAV VVIDVTQPIS VQDLNIIDLV LESGRALVIA
     YNKWDRLNDD DMDGQDRRRY LEREIEQDLA HVAWAPRVNI SARTGRHLDK LVPALETALE
     SWDQRIPTGK FNAFITELVA EHPHPVRGGK QPRILFGTQA STRPPTFVLF TSGFLDPGYR
     RFIQRRLREL YGFEGTPIVV NMRVRERRKR
//
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