HFLX_CHLPN
ID HFLX_CHLPN Reviewed; 472 AA.
AC Q9Z873; Q7AIQ8;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=GTPase HflX {ECO:0000255|HAMAP-Rule:MF_00900};
DE AltName: Full=GTP-binding protein HflX {ECO:0000255|HAMAP-Rule:MF_00900};
GN Name=hflX {ECO:0000255|HAMAP-Rule:MF_00900};
GN OrderedLocusNames=CPn_0478, CPj0478;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [3]
RP FUNCTION, INTERACTION WITH 50S SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, AND
RP MUTAGENESIS OF SER-243; THR-263 AND ASN-349.
RC STRAIN=CWL029;
RX PubMed=18957606; DOI=10.1099/mic.0.2008/022137-0;
RA Polkinghorne A., Ziegler U., Gonzalez-Hernandez Y., Pospischil A.,
RA Timms P., Vaughan L.;
RT "Chlamydophila pneumoniae HflX belongs to an uncharacterized family of
RT conserved GTPases and associates with the Escherichia coli 50S large
RT ribosomal subunit.";
RL Microbiology 154:3537-3546(2008).
CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit and may
CC have a role during protein synthesis or ribosome biogenesis. Specific
CC for GTP. {ECO:0000255|HAMAP-Rule:MF_00900,
CC ECO:0000269|PubMed:18957606}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00900};
CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit.
CC {ECO:0000255|HAMAP-Rule:MF_00900}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00900,
CC ECO:0000269|PubMed:18957606}. Note=May associate with membranes.
CC -!- DOMAIN: Full-length protein is required for specific association with
CC the 50S ribosomal subunit. {ECO:0000269|PubMed:18957606}.
CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC superfamily. HflX GTPase family. {ECO:0000255|HAMAP-Rule:MF_00900}.
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DR EMBL; AE001363; AAD18618.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA98684.1; -; Genomic_DNA.
DR PIR; B72073; B72073.
DR PIR; B86550; B86550.
DR RefSeq; NP_224674.1; NC_000922.1.
DR RefSeq; WP_010883116.1; NZ_LN847257.1.
DR AlphaFoldDB; Q9Z873; -.
DR SMR; Q9Z873; -.
DR STRING; 406984.CPK_ORF00993; -.
DR EnsemblBacteria; AAD18618; AAD18618; CPn_0478.
DR KEGG; cpj:hflX; -.
DR KEGG; cpn:CPn_0478; -.
DR PATRIC; fig|115713.3.peg.535; -.
DR eggNOG; COG2262; Bacteria.
DR HOGENOM; CLU_019597_1_0_0; -.
DR OrthoDB; 1592033at2; -.
DR Proteomes; UP000000801; Chromosome.
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; 3.40.50.11060; -; 1.
DR Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR10229; PTHR10229; 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; SSF52540; 1.
DR TIGRFAMs; TIGR03156; GTP_HflX; 1.
DR PROSITE; PS51705; G_HFLX; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; Magnesium; Metal-binding; Nucleotide-binding.
FT CHAIN 1..472
FT /note="GTPase HflX"
FT /id="PRO_0000412527"
FT DOMAIN 230..396
FT /note="Hflx-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 236..243
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 261..265
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 263
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 283..286
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 349..352
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT BINDING 374..376
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00900"
FT MUTAGEN 243
FT /note="S->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18957606"
FT MUTAGEN 263
FT /note="T->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18957606"
FT MUTAGEN 349
FT /note="N->Y: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18957606"
SQ SEQUENCE 472 AA; 52763 MW; 6DCF1A39F8F3BDB8 CRC64;
MDTIDTPGEQ GSQSFGNSLG ARFDLPRKEQ DPSQALAVAS YQNKTDSQVV EEHLDELISL
ADSCGISVLE TRSWILKTPS ASTYINVGKL EEIEEILKEF PSIGTLIIDE EITPSQQRNL
EKRLGLVVLD RTELILEIFS SRALTAEANI QVQLAQARYL LPRLKRLWGH LSRQKSGGGS
GGFVKGEGEK QIELDRRMVR ERIHKLSAQL KAVIKQRAER RKVKSRRGIP TFALIGYTNS
GKSTLLNLLT AADTYVEDKL FATLDPKTRK CVLPGGRHVL LTDTVGFIRK LPHTLVAAFK
STLEAAFHED VLLHVVDASH PLALEHVQTT YDLFQELKIE KPRIITVLNK VDRLPQGSIP
MKLRLLSPLP VLISAKTGEG IQNLLSLMTE IIQEKSLHVT LNFPYTEYGK FTELCDAGVV
ASSRYQEDFL VVEAYLPKEL QKKFRPFISY VFPEDCGDDE GRGPVLESSF GD
