ID   M4KYG2_BACIU            Unreviewed;       460 AA.
AC   M4KYG2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   13-NOV-2013, entry version 6.
DE   RecName: Full=GTPase HflX;
DE   AltName: Full=GTP-binding protein HflX;
GN   Name=ynbA; Synonyms=hflX; ORFNames=C663_1792;
OS   Bacillus subtilis XF-1.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1233100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=XF-1;
RX   PubMed=23558530;
RA   Guo S., Mao Z., Wu Y., Hao K., He P., He Y.;
RT   "Genome Sequencing of Bacillus subtilis Strain XF-1 with High
RT   Efficiency in the Suppression of Plasmodiophora brassicae.";
RL   Genome Announc. 1:E0006613-E0006613(2013).
CC   -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit
CC       and may have a role during protein synthesis or ribosome
CC       biogenesis (By similarity).
CC   -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=May associate with membranes
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the HflX GTPase family.
CC   -!- SIMILARITY: Contains 1 G (guanine nucleotide-binding) domain.
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DR   EMBL; CP004019; AGE63584.1; -; Genomic_DNA.
DR   RefSeq; YP_007426921.1; NC_020244.1.
DR   ProteinModelPortal; M4KYG2; -.
DR   EnsemblBacteria; AGE63584; AGE63584; C663_1792.
DR   GeneID; 14561883; -.
DR   KEGG; bsx:C663_1792; -.
DR   KO; K03665; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006184; P:GTP catabolic process; IEA:GOC.
DR   HAMAP; MF_00900; GTPase_HflX; 1; -.
DR   InterPro; IPR006073; GTP_binding_domain.
DR   InterPro; IPR016496; GTPase_HflX.
DR   InterPro; IPR025121; GTPase_HflX_N_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10229; PTHR10229; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Nucleotide-binding.
FT   DOMAIN      242    361       G (By similarity).
FT   NP_BIND     247    255       GTP (By similarity).
FT   NP_BIND     360    363       GTP (By similarity).
SQ   SEQUENCE   460 AA;  52450 MW;  B9C8A9195B8E0ADC CRC64;
     MRGLFFARIS AFQSNRFVVY TCRVWYDNTT AQYAKERNIH LNEQETIQEK AILVGCQLPH
     ITDEHFENSM EELASLTKTA DGKVLTSVTQ KRNRADAATY IGKGKVEELK ALVEELEADL
     LIFNDELSPS QLKSLATAIE VKMIDRTQLI LDIFAKRART REGKLQIELA QLQYALPRLT
     GQGINLSRQG GGIGARGPGE TKLETDRRHI RNRIHEINTQ LSTVIRHRSR YRERRKKNGV
     LQIALVGYTN AGKSTWFNRL TSADSYEEDL LFATLDPMTR KMVLPSGYSV LLSDTVGFIQ
     DLPTTLIAAF RSTLEEVKEA DLILHLIDSS NEDYAGHEKT VLRLLEELEA DDIPMLTAYN
     KRDQKLPDFI PSAGRDHIMV SAKFEDDAAA FKEAIQRYLR QELLTSFEAH VPASEGKLLS
     RIKSETMVDR FYFNEENEQY DISGYVQEEQ SIIGELKKYM
//