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Database: UniProt
Entry: A0A090IE13_9GAMM
LinkDB: A0A090IE13_9GAMM
Original site: A0A090IE13_9GAMM 
ID   A0A090IE13_9GAMM        Unreviewed;       451 AA.
AC   A0A090IE13;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900};
DE   AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900};
GN   Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900};
GN   ORFNames=MVIS_0900 {ECO:0000313|EMBL:CED58912.1};
OS   Moritella viscosa.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Moritellaceae; Moritella.
OX   NCBI_TaxID=80854 {ECO:0000313|EMBL:CED58912.1, ECO:0000313|Proteomes:UP000032438};
RN   [1] {ECO:0000313|Proteomes:UP000032438}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hjerde E.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit and may
CC       have a role during protein synthesis or ribosome biogenesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00900}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR006809-2};
CC   -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit.
CC       {ECO:0000256|HAMAP-Rule:MF_00900}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}.
CC       Note=May associate with membranes. {ECO:0000256|HAMAP-Rule:MF_00900}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC       superfamily. HflX GTPase family. {ECO:0000256|HAMAP-Rule:MF_00900}.
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DR   EMBL; LN554852; CED58912.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A090IE13; -.
DR   STRING; 80854.MVIS_0900; -.
DR   KEGG; mvs:MVIS_0900; -.
DR   PATRIC; fig|80854.5.peg.951; -.
DR   HOGENOM; CLU_019597_2_1_6; -.
DR   Proteomes; UP000032438; Chromosome complete sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd01878; HflX; 1.
DR   Gene3D; 6.10.250.2860; -; 1.
DR   Gene3D; 3.40.50.11060; GTPase HflX, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00900; GTPase_HflX; 1.
DR   InterPro; IPR030394; G_HFLX_dom.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR032305; GTP-bd_M.
DR   InterPro; IPR016496; GTPase_HflX.
DR   InterPro; IPR025121; GTPase_HflX_N.
DR   InterPro; IPR042108; GTPase_HflX_N_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR03156; GTP_HflX; 1.
DR   PANTHER; PTHR10229:SF0; GTP-BINDING PROTEIN 6-RELATED; 1.
DR   PANTHER; PTHR10229; GTP-BINDING PROTEIN HFLX; 1.
DR   Pfam; PF16360; GTP-bdg_M; 1.
DR   Pfam; PF13167; GTP-bdg_N; 1.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1.
DR   PRINTS; PR00326; GTP1OBG.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51705; G_HFLX; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00900};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR006809-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR006809-2};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00900}; Reference proteome {ECO:0000313|Proteomes:UP000032438}.
FT   DOMAIN          229..398
FT                   /note="Hflx-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51705"
FT   BINDING         235..242
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT   BINDING         242
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006809-2"
FT   BINDING         260..264
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT   BINDING         262
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006809-2"
FT   BINDING         282..285
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT   BINDING         348..351
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
FT   BINDING         372..374
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006809-1"
SQ   SEQUENCE   451 AA;  50641 MW;  4A70AD4C1FADBB54 CRC64;
     MSTDMSITTT EHSVTRALLI SIRTPCTTQQ DVDESLSELG RLVHTLGFSV VGTKTQRQKS
     TKQLSVLGAG KLEELASLTG ESTFYEDEVQ IELDQDELSQ LLATTDVKCQ ANIVVFDCEL
     SPNQLSNVKA ALGVEVYDRT RVIIEIFSKH ARTRTAKLQV EIARLNYLTP RLRDESSGDR
     ERQKGRSISE TVFEINRRRV RTKIAELRRE LTKVQREMQG RSSGRIEQLT VALVGYTNAG
     KSSLMRALTG SEVLVEDKLF ATLDTTIRTL QPPTQPRILI SDTVGFIQKL PHDLVASFHS
     TLEEAKNADL LLYVVDASDE NFISQLAIVD HVLGQLNIDL NNKVLLLNKV DCLNEEQQLD
     LLERYPDALQ ISAHDKGDVA FVHQEIQNLL EKKMCPACFD IPYTASGVIG EIHSKMQVLE
     EEYHEKGIRI TLKASPVALE RLHKMLQLTT F
//
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