ID A0A2P8WFI5_9CYAN Unreviewed; 560 AA.
AC A0A2P8WFI5;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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 ECO:0000313|EMBL:PSN18575.1};
GN ORFNames=C7271_11800 {ECO:0000313|EMBL:PSN18575.1};
OS filamentous cyanobacterium CCP5.
OC Bacteria; Cyanobacteriota.
OX NCBI_TaxID=2107701 {ECO:0000313|EMBL:PSN18575.1, ECO:0000313|Proteomes:UP000240885};
RN [1] {ECO:0000313|EMBL:PSN18575.1, ECO:0000313|Proteomes:UP000240885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCP5 {ECO:0000313|EMBL:PSN18575.1,
RC ECO:0000313|Proteomes:UP000240885};
RA Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT "The ancient ancestry and fast evolution of plastids.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000240885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCP5 {ECO:0000313|Proteomes:UP000240885};
RA Moore K., Momper L.;
RL Submitted (MAR-2018) 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 -!- 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}.
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:PSN18575.1}.
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DR EMBL; PYEQ01000196; PSN18575.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8WFI5; -.
DR OrthoDB; 9812272at2; -.
DR Proteomes; UP000240885; Unassembled WGS 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 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}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00900}; Reference proteome {ECO:0000313|Proteomes:UP000240885}.
FT DOMAIN 389..558
FT /note="Hflx-type G"
FT /evidence="ECO:0000259|PROSITE:PS51705"
FT REGION 333..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 560 AA; 61872 MW; 0790892282B03E29 CRC64;
MDTVHGHLQG LKPSQLKQLQ RLYHQRIPGD RITTPEFAQR LAAISTEINQ PVCTYINRRG
QVVRVGVGTP QKTQIPPLEL PRYGAERLCG IRCLATQLKP DPPSESALTA MAIQRLDALA
LLTLSGGGFQ RRGGGATGYV KSAYLAHLVP SVEERWSVSP ATSLDVLAKQ DFLDLAEGLE
AEFRREFVAR QVDIDHDRVL MVGLMIASQT KDQFHARMNE LRRLVESAGG DVLGSLDQRR
SRPHPQTVLG AGKVQEVALA VQTLGANLVV CDRDLSPAQV RNLENRIGVR VVDRTELILD
IFAQRAKTGA GKLQVELAQL EYQLPRLTGR GQAMSRLGGG IGTRGPGETK LETERRSIQR
RITRLQQEVN QLQAHRARLR QRRQHDDVPS IAVVGYTNAG KSTLVNTLTN SEVYAADQLF
ATLDPTTRRL SILDESDTPR GLVVTDTVGF IEELPPPLMD AFRATLEEVT EADALLHVVD
ISHPAWQAQI HAVMNLLQAL PMTSGPILLV FNKADRVDRD QLVLAQEEYP QAIFVSATQR
LGLETLRLKL LQLVDYAVAV
//
